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J Mol Biol 272:348–361. https:\u002F\u002Fdoi.org\u002F10.1006\u002Fjmbi.1997.1245\nAlves CQ et al (2013) In vitro acetylcholinesterase activity of peptide derivatives isolated from two species of Leguminosae. Pharm Biol 51:936–939\nAmblard M, Fehrentz JA, Martinez J, Subra G (2006) Methods and protocols of modern solid phase peptide synthesis. Mol Biotechnol 33:239–254. https:\u002F\u002Fdoi.org\u002F10.1385\u002Fmb:33:3:239\nAno Y, Ayabe T, Ohya R, Kondo K, Kitaoka S, Furuyashiki T (2019) Tryptophan-tyrosine dipeptide, the core sequence of β-lactolin, improves memory by modulating the dopamine system. Nutrients 11:348\nAlzheimer's Association (2018) Alzheimer's disease facts and figures. Alzheimers Dement 14:367–429\nBajda M et al (2020) Search for new multi-target compounds against Alzheimer’s disease among histamine H3 receptor ligands. Eur J Med Chem 185:111785\nBechara C, Sagan S (2013) Cell-penetrating peptides: 20 years later, where do we stand? FEBS Lett 587:1693–1702\nBolognesi ML, Cavalli A (2016) Multitarget drug discovery and polypharmacology. ChemMedChem 11:1190–1192\nBourne Y, Taylor P, Marchot P (1995) Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex. Cell 83:503–512\nBussi G, Donadio D, Parrinello M (2007) Canonical sampling through velocity rescaling. J Chem Phys 126:014101\nCraig LA, Hong NS, McDonald RJ (2011) Revisiting the cholinergic hypothesis in the development of Alzheimer's disease. Neurosci Biobehav Rev 35:1397–1409\nCummings JL (2004) Alzheimer’s disease. N Engl J Med 351:56–67\nDastan D, Validi S, Ebadi A (2020) Kamonolol acetate from Ferula pseudalliacea as AChE inhibitor: in vitro and in silico studies. Struct Chem. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs11224-019-01473-z\nDe Ferrari GV, Canales MA, Shin I, Weiner LM, Silman I, Inestrosa NC (2001a) A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation. Biochemistry 40:10447–10457. https:\u002F\u002Fdoi.org\u002F10.1021\u002Fbi0101392\nDe Ferrari GV, Canales MA, Shin I, Weiner LM, Silman I, Inestrosa NC (2001b) A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation. Biochemistry 40:10447–10457\nEllman GL, Courtney KD, Andres V Jr, Featherstone RM (1961) A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 7:88–95\nFalkenstein RJ, Pena C (1999) Interaction of synthetic peptides from fasciculin with acetylcholinesterase. J Protein Chem 18:233–238\nFalkenstein RJ, Peña C (1997) Synthetic peptides derived from the central loop of fasciculin: structural analysis and evaluation as inhibitors of acetylcholinesterase. Biochim Biophys Acta 1340:143–151\nFosgerau K, Hoffmann T (2015) Peptide therapeutics: current status and future directions. Drug Discov Today 20:122–128\nHampel H et al (2019) Revisiting the cholinergic hypothesis in Alzheimer’s disease: emerging evidence from translational and clinical research. J Prev Alzheimers Dis 6:2–15\nHampel H et al (2018) The cholinergic system in the pathophysiology and treatment of Alzheimer’s disease. Brain 141:1917–1933\nHess B, Kutzner C, Van Der Spoel D, Lindahl E (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4:435–447\nInestrosa NC et al (1996) Acetylcholinesterase accelerates assembly of amyloid-beta-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 16:881–891. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fs0896-6273(00)80108-7\nKortemme T, Baker D (2002) A simple physical model for binding energy hot spots in protein–protein complexes. Proc Natl Acad Sci 99:14116–14121\nLaskowski RA, Jabłońska J, Pravda L, Vařeková RS, Thornton JM (2018) PDBsum: structural summaries of PDB entries. Protein Sci 27:129–134\nMondal P, Gupta V, Das G, Pradhan K, Khan J, Gharai PK, Ghosh S (2018) Peptide-based acetylcholinesterase inhibitor crosses the blood-brain barrier and promotes neuroprotection. ACS Chem Neurosci 9:2838–2848\nNachon F, Carletti E, Ronco C, Trovaslet M, Nicolet Y, Jean L, Renard P-Y (2013) Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl-and butyryl-cholinesterase. Biochem J 453:393–399\nParrinello M, Rahman A (1981) Polymorphic transitions in single crystals: a new molecular dynamics method. J Appl Phys 52:7182–7190\nParthasarathy A, Anandamma SK, Kalesh KA (2019) The medicinal chemistry of therapeutic peptides: recent developments in synthesis and design optimizations. Curr Med Chem 26(13):2330–2355\nRadić Z, Duran R, Vellom DC, Li Y, Cervenansky C, Taylor P (1994) Site of fasciculin interaction with acetylcholinesterase. J Biol Chem 269:11233–11239\nRazzaghi-Asl N, Ebadi A (2020) In silico design of peptide inhibitors of tubulin: amyloid-β as a lead compound. J Biomol Struct Dyn. https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1764391\nSaxena A, Saini R (2018) The structural hybrids of acetylcholinesterase inhibitors in the treatment of Alzheimer’s disease: a review. J Alzheimers Neurodegener Dis 4:015\nSelkoe DJ, Hardy J (2016) The amyloid hypothesis of Alzheimer's disease at 25 years. EMBO Mol Med 8:595–608\nVan Zundert G et al (2016) The HADDOCK2.2 web server: user-friendly integrative modeling of biomolecular complexes. J Mol Biol 428:720–725\nWaqar M, Batool S (2015) In silico analysis of binding of neurotoxic venom ligands with acetylcholinesterase for therapeutic use in treatment of Alzheimer's disease. J Theor Biol 372:107–117. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jtbi.2015.02.028\nWilson RS, Segawa E, Boyle PA, Anagnos SE, Hizel LP, Bennett DA (2012) The natural history of cognitive decline in Alzheimer's disease. Psychol Aging 27:1008\nYu Z et al (2018) Anti-Alzheimers activity and molecular mechanism of albumin-derived peptides against AChE and BChE. Food Funct 9:1173–1178\nZare-Zardini H, Tolueinia B, Hashemi A, Ebrahimi L, Fesahat F (2013) Antioxidant and cholinesterase inhibitory activity of a new peptide from Ziziphus jujuba fruits. Am J Alzheimers Dis Other Demen 28:702–709. https:\u002F\u002Fdoi.org\u002F10.1177\u002F1533317513500839",{"EN":149},"Alzheimer’s disease (AD) is an irreversible and progressive brain disorder that slowly destroys memory and cognitive skills. The current treatment of AD mainly focused on the restoring of ACh levels through acetylcholinesterase (AChE) inhibition. Peptides are a unique class of pharmaceutical compounds that have privilege over small molecules, especially in the realm of protein–protein interactions and G protein-coupled receptor (GPCR) inhibitors. We applied a rational structure-based virtual design approach to discover new peptidic inhibitors of AChE. In this regard, conformational space in the fasciculin II (Fas) and AChE complex was evaluated utilizing MD simulation, principal component analysis and clustering to figure out possible interactions of Fas and AChE. Assessment of Fas–AChE interactions by visual evaluation and alanine scanning led to the design of 10 peptides. The highest scored peptide (p2) was selected and synthesized using SPPS. Based on Ellman's test, the inhibitory activity of p2 against AChE was 51.2 ± 8.1 µM. The kinetics study of the enzyme inhibition in accompany with molecular modeling results revealed that p2 was a mixed-type reversible inhibitor of AChE. The DNRMLRTTRY peptide was considerable inhibitor of AChE. Peptides have the merit of being big enough to inhibit PPI and GPCR class B with a wide binding site. But possible peptidic chemical space is too large to be evaluated by the classical peptide synthesis methods. In the present contribution, we introduced a rational in silico peptide design approach that led to the considerable peptidic inhibitor of AChE.",{"EN":151},"From Venom to AChE Inhibitor: Design, Molecular Modeling, and Synthesis of a Peptidic Inhibitor of AChE",{"VOID":153},"10.1007\u002Fs10989-020-10103-w","PUBLICATION","VERIFIED","Auto Verify","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10989-020-10103-w",[159,175,191],{"id":160,"sortIndex":21,"researcher":20,"roles":161,"affiliations":163,"properties":172},"589c5786-5868-4678-bfa7-ba2af264d995",[162],"AUTHOR",[164],{"id":20,"sortIndex":21,"affiliation":165,"properties":20},{"id":166,"createTime":167,"updateTime":167,"relativeEntities":168,"slug":20,"properties":169,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"65a31374-dbb8-4c14-81fb-01c9db0632a2","2023-12-24T23:58:18.102+00:00",[],{"title":170},{"VI":171},"Department of Pharmacognosy, School of Pharmacy, Medicinal Plants and Natural Products Research Center, Hamadan University of Medical Sciences, Hamadan, Iran",{"title":173},{"VI":174},"Dara Dastan",{"id":176,"sortIndex":177,"researcher":20,"roles":178,"affiliations":179,"properties":188},"867a527e-aa00-4058-a6f5-84da0e6a0177",2,[162],[180],{"id":20,"sortIndex":21,"affiliation":181,"properties":20},{"id":182,"createTime":183,"updateTime":183,"relativeEntities":184,"slug":20,"properties":185,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"9b7cc5d6-0c45-4584-94bd-9c1cef34e4ff","2024-01-12T17:27:57.668+00:00",[],{"title":186},{"VI":187},"Department of Medicinal Chemistry, School of Pharmacy, Medicinal Plants and Natural Products Research Center, Hamadan University of Medical Sciences, Hamadan, Iran",{"title":189},{"VI":190},"Ahmad Ebadi",{"id":192,"sortIndex":131,"researcher":20,"roles":193,"affiliations":194,"properties":200},"e884436c-8233-4e7d-8c7d-2678bbdf7e9c",[162],[195],{"id":20,"sortIndex":21,"affiliation":196,"properties":20},{"id":182,"createTime":183,"updateTime":183,"relativeEntities":197,"slug":20,"properties":198,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":199},{"VI":187},{"title":201},{"VI":202},"Kiana Fasihi","ARTICLE",{"url":157,"publisher":205,"properties":233},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":206,"slug":10,"properties":207,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":211,"manageAffiliations":212,"indexDatabases":213,"url":20,"thumbnailPath":20,"statistic":228,"gsStatistic":20,"type":20,"analyzePriority":20},[],{"issn":208,"eissn":209,"title":210},{"VOID":13},{"VOID":15},{"EN":17},[],[],[214,221],{"id":88,"indexDatabase":215,"url":103,"indexYears":20,"academicFieldIds":220,"indexDatabaseRanking":20},{"id":90,"createTime":91,"updateTime":92,"relativeEntities":216,"label":217,"description":218,"key":99,"publicationTags":219,"standard":20},[],{"EN":95,"VI":95},{"VI":97,"EN":98},[101,102],[105],{"id":107,"indexDatabase":222,"url":120,"indexYears":121,"academicFieldIds":227,"indexDatabaseRanking":128},{"id":109,"createTime":110,"updateTime":111,"relativeEntities":223,"label":224,"description":225,"key":117,"publicationTags":226,"standard":20},[],{"EN":114,"VI":114},{"EN":114,"VI":116},[119],[123,124,125,126,127],{"impactFactor":21,"impactFactorByYear":229,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":131,"totalPublicationByYear":230,"totalCitation":21,"totalCitationByYear":231,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":232,"hindexLast5Year":21,"hindex":21},{},{"2020":131},{},{},{"volume":234,"pages":236},{"VOID":235},"27",{"VOID":237},"463-474","2020-07-21",2020,false,{"id":242,"createTime":243,"updateTime":244,"relativeEntities":245,"slug":246,"properties":247,"entityType":154,"verifyStatus":155,"verifyTime":244,"verifyNote":156,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":256,"fullTextUrl":20,"authors":257,"publicationType":203,"publisherRelationship":346,"citationCount":20,"citationInfo":20,"publishDate":380,"publishYear":381,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":20,"openAccess":20,"references":20,"isForceReanalyzing":240},"0babd16f-a82b-47b3-a057-c77a1ff744fd","2024-02-07T08:33:00.247+00:00","2025-01-22T23:57:35.570+00:00",[],"Improvement-of-the-Antioxidant-Activity-of-Fenugreek-Protein-Isolates-by-Lactococcus-lactis-Fermentation",{"references":248,"abstract":250,"title":252,"doi":254},{"VOID":249},"Aguirre I, Garro MS, de Giori G (2008) Enzymatic hydrolysis of soybean protein using lactic acid bacteria. Food Chem 4:976–982\nAgyei D, Ongkudon CM, Yi Wei C, Chan AS, Danquah MK (2016) Bioprocess challenges to the isolation and purification of bioactive peptides. Food Bioprod. Process. 98:244–256\nAOAC (1990). Official methods of analysis (15th edn). Association of Official Analytical Chemists. Washington\nBelguith-Hadriche O, Bouaziz M, Jamoussi K, Simmonds MSJ, El Feki A, Makni-Ayedi F (2013) Comparative study on hypocholesterolemic and antioxidant activities of various extracts of fenugreek seeds. Food Chem 138:1448–1453\nBengoechea C, Romero A, Villanueva A, Moreno G, Alaiz F, Milla A, Guerrero PC (2008) Composition and structure of carob (Ceratonia siliqua L.). Germ Proteins Food Chem 107:675–683\nBillaud C, Adrian J (2001) Le fenugrec: composition, valeur nutritionnelle et physiologique. Sci Des Aliment. 21, 3–26\nDakia PA, Wathelet B, Paquot M (2007) Isolation and chemical evaluation of carob (Ceratonia siliqua L.). Food Chem 102:1368–1374\nDei Piu’ L, Tassoni A, Serrazanetti A, Ferri DI, Babini M, Tagliazucchi E, Gianotti D A (2014) Exploitation of starch industry liquid by-product to produce bioactive peptides from rice hydrolyzed proteins. Food Chem 155:199–206\nDurak A, Baraniak B, Jakubczyk A, Swieca M (2013) Biologically active peptides obtained by enzymatic hydrolysis of Adzuki been seeds. Food Chem 141:2177–2183\nEl Nasri Nazar A, El Tinay AH (2007) Functional properties of fenugreek (Trigonella foenum graecum) protein concentrate. Food Chem 103:582–589\nFadda S, Lopez C, Vignolo G (2010) Role of lactic acid bacteria during meat conditioning and fermentation: peptides generatedas sensorial and hygienic biomarkers. Meat Sci 86:66–79\nHamdi M, Lengliz S, Kachouri F, Bouzouita N, Fraj B, Malek A (2008) Procédé enzymatique et chimique d’extraction de la gomme du fenugrec et récupération d’extraits protéiques et de fibres alimentaires. Brevet tunisien N°SN 08013\nHe R, Girgih AT, Malomo SA, Ju X, Aluko RE (2013) Antioxidant activities of enzymatic rapeseed protein hydrolysates and the membrane ultrafiltration fractions. J Funct Foods 5:219–227\nKachouri F, Ksontini H, Kraiem M, Setti K, Mechmeche M, Hamdi M (2015) Involvement of antioxidant activity of Lactobacillus plantarum on functional properties of olive phenolic compounds. J Food Sci Technol 52:7924–7933\nKaviarasan S, Naik GH, Gangabhagirathi R, Anuradha CV, Priyadarsini KI (2007) In vitro studies on antiradical and antioxidant activities of fenugreek (Trigonella foenum-graecum) seeds. Food Chem 103:31–37. doi:10.1016\u002Fj.foodchem.2006.05.064\nKhole S, Chatterjee S, Variyar P, Sharma A, Devasagayam T.P.A., Ghaskadbi S (2014) Bioactive constituents of germinated fenugreek seeds with strong antioxidant potential. J Funct Foods 6:270–279\nKong X, Zhou H, Qian H (2006) Enzymatic hydrolysis of wheat gluten by proteases and properties of the resulting hydrolysates. Food Chem 102:759–763\nKorhonen H, Pihlanto A (2006) Bioactive peptides: production and functionality. Int Dairy J 16:945–960\nLaemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685\nMirzaei M, Mirdamadi S, Ehsani MR, Aminlari M (2016) Antioxidant, ACE-Inhibitory and antibacterial activities of Kluyveromyces marxianus protein hydrolysates and their peptide fractions. Funct Foods Health Dis 6(7):425–439\nNaidu MM, Shyamala BN, Pura Naik J, Sulochanamma G, Srinivas P (2011) Chemical composition and antioxidant activity of the husk and endosperm of fenugreek seeds. LWT—Food Sci Technol 44:451–456. doi:10.1016\u002Fj.lwt.2010.08.013\nRe R, Pellegrini N, Proteggente A, Pannala A, Yang M, Rice-Evans C (1999) Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radic Bio Med 26:1231–1237\nSamarzija D, Antunac N, Havranek JL (2001) Taxonomy, physiology and growth of Lactococcus lactis: a review. Mljekarstvo 51:35–48\nSarmadia BH, Ismaila A (2010) Antioxidative peptides from food proteins. Peptides 31, 1949–1956\nSheih I, Wu T, Fang T (2009) Antioxidant properties of a new antioxidative peptide from algae protein waste hydrolysate in different oxidation systems. Bioresour Technol 100:3419–3425\nYu J, Hu Y, Xue M, Dun Y, Li S, Peng N, Liang Y, Zhao S (2016) Purification and identification of antioxidant peptides from enzymatic hydrolysate of Spirulina platensis. J Microbiol Biotechnol 26(7):1216–1223\nZhou C, Hu J, Ma H, Yagoub AE, Yu X, Owusu J, Ma H, Qin X (2015) Antioxidant peptides from corn gluten meal: orthogonal design evaluation. Food Chem 187:270–278\nZiadi M, Bergot G, Courtin P, Chambellon E, Hamdi M, Yvon M (2009). Amino acid catabolism by Lactococcus lactis during milk fermentation. Int Dairy J, 1–7",{"EN":251},"This study investigated the antioxidant capacity of fenugreek protein isolate and its improvement by Lc. lactis fermentation through bioactive peptides production and the effect of molecular weight variation on fenugreek fractions antioxidant activity. Fenugreek protein isolate showed a significant increase of antioxidant and radical scavenging activity after 24 h of fermentation, by about 23.7, 42.9 and 40% for respectively antioxidant activity coefficient AAC, DPPH and ABTS radical scavenging activity. FI fermentation led to a hydrolysis of peptide bands with MW > 35 kDa and a generation of new bands with a MW \u003C 25 kDa. A significant reduction in molecular-mass distribution of hydrolysates and a great increase of total free amino acids content, especially an increase on isoleucine, leucine, glutamic acid, serine, histidine, glutamine and lysine was noted. The infrared results showed that different reactions may take place after fermentation, and showed an increase of proteins, amides and aromatic compounds. However, fenugreek fraction (F2) with MW 15–50 kDa presented the highest activity instead of fraction (F1) with lower MW. Lc. lactis had the ability to degrade and convert fenugreek proteins into bioactive peptides that contribute positively in the improvement of antioxidant activity of FI and fractions. FI presents a significant antioxidant activity and thus, can be considered as a potential source of high added value natural antioxidants and may be employed as a functional food ingredient with good potential applications in food products.",{"EN":253},"Improvement of the Antioxidant Activity of Fenugreek Protein Isolates by Lactococcus lactis 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Tunis, Tunisia",{},{"title":292},{"VI":293},"Khaoula 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D, Khalil Z, Satkunanthan N, Livett B (2003) Drugs from the sea: conotoxins as drug leads for neuropathic pain and other neurological conditions. Mini Rev Med Chem 3:785–787\nAnanthan G, Karthikeyan MM, Selva PA, Raghunathan C (2012) Studies on the seasonal variations in the proximate composition of ascidians from the Palk Bay, southeast coast of India. Asian Pac J Trop Biomed 2(10):793–797\nArumugam V, Venkatesan M, Ramachandran S, Sundaresan U (2018) Bioactive peptides from marine ascidians and future drug development—a review. Int J Pept Res Ther 24(1):13–18\nAzumi K, Yokosawa H, Ishii S (1990) Halocyamines: novel antimicrobial tetrapeptide-like substances isolated from the hemocytes of the solitary ascidian Halocynthia roretzi. Biochemistry 29(1):159–165\nBalachandar R, Karmegam N, Saravanan M, Subbaiya R, Gurumoorthy P (2018) Synthesis of bioactive compounds from vermicast isolated actinomycetes species and its antimicrobial activity against human pathogenic bacteria. Microb Pathog 121:155–165\nBarabadi H, Alizadeh A, Ovais M, Ahmadi A, Shinwari ZK, Saravanan M (2017a) Efficacy of green nanoparticles against cancerous and normal cell lines: a systematic review and meta-analysis. IET Nano Biotechnol 12(4):377–391\nBarabadi H, Ovais M, Shinwari ZK, Saravanan M (2017b) Anti-cancer green bionanomaterials: present status and future prospects. Green Chem Lett Rev 10(4):285–314\nBradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72(1–2):248–254\nCarroll AR, Feng Y, Bowden BF, Coll JC (1996a) Studies of Australian ascidians. 5. Virenamides A–C, new cytotoxic linear peptides from the colonial Didemnid ascidian Diplosoma virens. J Org Chem 61(12):4059–4061\nCarroll AR, Coll JC, Bourne DJ, MacLeod JK, Zabriskie TM, Ireland CM, Bowden BF (1996b) Patellins 1–6 and Trunkamide A: Novel Cyclic Hexa-, Hepta-and Octa-peptides from colonial ascidians, Lissoclinum sp. AUST J CHEM 49(6):659–667\nDavidson BS (1993) Ascidians: producers of amino acid derived metabolites. Chem Rev 93:1771–1791\nDonia MS, Wang B, Dunbar DC, Desai PV, Patny A, Avery M, Hamann MT (2008) Mollamides B and C, cyclic hexapeptides from the Indonesian tunicate Didemnum molle. J Nat Prod 71(6):941–945\nFang WY, Dahiya R, Qin HL, Mourya R, Maharaj S (2016) Natural proline-rich cyclopolypeptides from marine organisms: chemistry, synthetic methodologies and biological. Status Mar Drugs 14(11):194\nFenical W (1974) Proceedings of the food-drugs from the sea conference, Marine Science Center, University of Puerto Rico; Mayaguez, Puerto Rico. Marine Technology Society, Washington, DC, 388\nGalinier R, Roger E, Sautiere PE, Aumelas A, Banaigs B, Mitta G (2009) Halocyntin and papillosin, two new antimicrobial peptides isolated from hemocytes of the solitary tunicate, Halocynthia papillosa. Journal of Peptide Science 15(1):48–55\nGaridel P, Schott H (2006) Fourier-transform midinfrared spectroscopy for analysis and screening of liquid protein formulations. Bioprocess Int 4(6):48–55\nIreland CM, Fernandez A (1996) Cyclic peptide antitumor agent from an ascidian. US 5830996 A\nIreland C, Scheuer PJ (1990) Ulicyclamide and ulithiacyclamide, two new small peptides from a marine tunicate. J Am Chem Soc 102(17):5688–5691\nJang WS, Kim KN, Lee YS, Nam MH, Lee IH (2002a) Halocidin: a new antimicrobial peptide from hemocytes of the solitary tunicate, Halocynthia aurantium. FEBS Lett 521:81–86\nJang WS, Kim KN, Lee YS, Nam MH, Lee IH (2002b) Halocidin: a new antimicrobial peptide from hemocytes of the solitary tunicate, Halocynthia aurantium. FEBS Lett 521(1–3):81–86\nKarthik R, Saravanan R, Ebenezar KK, Sivamalai T (2015) Isolation, purification and characterization of avian antimicrobial glycopeptide from the posterior salivary gland of Sepia pharaonis. Appl Biochem Biotechnol 175:1507–1518\nKarthik R, Manigandan V, Saravanan R, Rajesh RP, Baby C (2016) Structural characterization and in vitro biomedical activities of sulfated chitosan from Sepia pharaonis. Int J Biol Macromol 31(8):9–32\nKim SK, Wijesekara I (2010) Development and biological activities of marine-derived bioactive peptides: a review. J Funct Foods 2:1–9\nKossuga MH, Lira SP, McHugh S, Torres YR, Lima BA, Gonçalves R, Veloso K, Ferreira AG, Rocha RM, Berlinck RG (2009) Antibacterial modified diketopiperazines from two ascidians of the genus Didemnum. J Braz Chem Soc 20(4):704–711\nLee IH, Zhao C, Cho Y, Harwig SS, Cooper EL, Lehrer RI (1997) Clavanins, α-helical antimicrobial peptides from tunicate hemocytes. Febs Lett 400(2):158–162\nLee IH, Lee YS, Kim CH, Kim CR, Hong T, Menzel L, Boo LM, Pohl J, Sherman MA, Waring A, Lehrer RI (2001a) Dicynthaurin: an antimicrobial peptide from hemocytes of the solitary tunicate, Halocynthia aurantium. Biochimica et Biophysica Acta (BBA)-General Subjects. 1527(3):141–148\nLee IH, Zhao C, Nguyen T, Menzel L, Waring AJ, Sherman MA, Lehrer RI (2001b) Clavaspirin, an antimicrobial and hemolytic peptide from Styela clava. J Peptide Res 58:445–456\nLi B, Webster TJ (2018) Bacteria antibiotic resistance: new challenges and opportunities for implant-associated orthopedic infections. J Orthop Res 36(1):22–32\nLighezan L, Georgieva R, Neagu A (2016) the secondary structure and the thermal unfolding parameters of the S-layer protein from Lactobacillus salivarius. Eur Biophys J45(6):491–509\nLordan S, Ross RP, Stanton C (2011) Marine bioactives as functional food ingredients: potential to reduce the incidence of chronic diseases. Mar Drugs 9(6):1056–1100\nMayer AMS, Glaser KB, Cuevas C (2010) The odyssey of marine pharmaceuticals: a current pipeline perspective. Trends Pharmacol Sci 31:255–265\nMcKinney ML, Schoch RM, Yonavjak L (2007) Environmental science: systems and solutions, 4th edn. Jones and Bartlett Publishers, Sudbury: 2007\nNaumann D, Helm D, Labischinski H, Giesbrecht P (1991) the characterisation of microorganisms by Fourier-transform infrared spectroscopy (FT-IR). In: Nelson WH (ed) Modern techniques for rapid microbiological analysis. VCH Publishers, New York, pp 43–96\nOvais M, Khalil AT, Raza A, Khan MA, Ahmad I, Islam NU, Saravanan M, Ubaid MF, Ali M, Shinwari ZK (2016) Green synthesis of silver nanoparticles via plant extracts: beginning a new era in cancer theranostics. Nanomedicine 12(23):3157–3177\nOvais M, Khalil AT, Raza A, Islam NU, Ayaz M, Saravanan M, Ali M, Ahmad I, Shahid M, Shinwari ZK (2018) Multifunctional theranostic applications of biocompatible green-synthesized colloidal nanoparticles. Appl Microbiol Biotechnol (10):4393–408\nPalanisamy SK, Rajendran NM, Marino A (2017) Natural products diversity of marine ascidians (tunicates; ascidiacea) and successful drugs in clinical development. Nat Prod Bioprospect 7(1):1–111\nPalanisamy SK, Arumugam V, Rajendran S, Ramadoss A, Nachimuthu S, Peter DM, Sundaresan U (2018) Chemical diversity and anti-proliferative activity of marine algae. Nat Prod Res 25:1–5\nPfalzgraff A, Brandenburg K, Weindl G (2018) Antimicrobial peptides and their therapeutic potential for bacterial skin infections and wounds. Front Pharmacol 9:281\nPhyo Y, Ribeiro J, Fernandes C, Kijjoa A, Pinto M ((2018) Marine natural peptides: determination of absolute configuration using liquid chromatography methods and evaluation of bioactivities. Molecules 23(2):306\nRinehart KL (2000) Antitumor compounds from tunicates. Med res rev 20(1):1–27\nSambrook J, Russell DW (2006) SDS-polyacrylamide gel electrophoresis of proteins. CSH Protoc 2006(4):pdb.prot4540\nSaravanan M, Barik SK, MubarakAli D, Prakash P, Pugazhendhi A (2018a) Synthesis of silver nanoparticles from Bacillus brevis (NCIM 2533) and their antibacterial activity against pathogenic bacteria. Microb Pathog 116:221–226\nSaravanan M, Arokiyaraj S, Lakshmi T, Pugazhendhi A (2018b) Synthesis of silver nanoparticles from Phenerochaete chrysosporium (MTCC-787) and their antibacterial activity against human pathogenic bacteria. Microb Pathog 117:68–72\nSaravanan M, Ramachandran B, Barabadi H (2018c) The prevalence and drug resistance pattern of extended spectrum β–lactamases (ESBLs) producing Enterobacteriaceae in Africa. Microbial Pathog 114:180–192\nShenkar N, Swalla BJ (2011) Global diversity of Ascidiacea. PLoS ONE 6(6):e20657\nTincu JA, Taylor SW (2004) Antimicrobial peptides from marine invertebrates. Antimicrob Agents Chemother 48(10):3645–3654\nTincu JA, Craig AG, Taylor SW (2000) Plicatamide: a lead to the biosynthetic origins of the tunichromes? Biochem Biophys Res Commun 70(2):421–424\nUeda A, Suzuki M, Honma T, Nagai H, Nagashima Y, Shiomi K (2006) Purification, properties and cDNA cloning of neoverrucotoxin (neoVTX), a hemolytic lethal factor from the stonefish Synanceia verrucosa venom. Biochim Biophy Acta 1760(11):1713–1722\nWallace BA (2009) Protein characterisation by synchrotron radiation circular dichroism spectroscopy. QRev Biophys 42:317–370\nXing H, Tong M, Jiang N, Zhang X, Hu H, Pan H, Li D (2017) Antitumour bioactive peptides isolated from marine organisms. Clin Exp Pharmacol Physiol 44(11):1077–1082",{"EN":392},"Marine ecosystems are unique and a largely diverse chest of natural resources which are still to be explored for new marine species. They are still unexplored for their pharmacological properties. Ascidians or sea squirts are invertebrate and fruitful candidate of a wide variety of biologically active secondary metabolites from cyclic peptides to aromatic alkaloids. In this study, we have purified peptides through isolation with buffer assay method and purification method by RP-HPLC. The molecular weight of purified ascidian peptide P1 was determined through the SDS-PAGE analysis and confirmed the molecular weight below 40 kDa. The purified peptides P1 were characterized by Fourier Transform Infrared spectroscopy (FTIR) and Circular Dichroism (CD) analysis. The purified peptides P1 confirmed by peaks at 555.82 (Amide VI), 642.12 (Amide V), 674.17 (Amide IV), 1527.19 (Amide II), 3281.97 (Amide A) and CD spectrum showed the positive peaks at 196 nm and two negative peaks at 193 and 199 nm, which is characteristic of the presence of a helical confirmation presence of peptides. The purified peptides P1 demonstrated the antibacterial activity against the highest inhibition reported the gram-positive bacteria, E. faecalis (11.60 ± 0.16 mm) and lowest inhibition shown the gram negative bacteria, P. aeruginosa (10.33 ± 0.12 mm) in 100 µg\u002Fml concentration. The present study was concluded that purified peptides of the ascidian, Didemnum sp. has a potential antibacterial effect against human pathogens.",{"EN":394},"Purification, Characterization and Antibacterial Properties of Peptide from Marine Ascidian Didemnum sp.",{"VOID":396},"10.1007\u002Fs10989-019-09829-z","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10989-019-09829-z",[399,415,427,443,468,480],{"id":400,"sortIndex":401,"researcher":20,"roles":402,"affiliations":403,"properties":412},"05916735-475a-4aa8-9681-e37e4cd837ee",5,[162],[404],{"id":20,"sortIndex":21,"affiliation":405,"properties":20},{"id":406,"createTime":407,"updateTime":407,"relativeEntities":408,"slug":20,"properties":409,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"a86f5960-a7f9-4696-bfa1-7d0be77947eb","2024-01-01T12:20:30.817+00:00",[],{"title":410},{"VI":411},"Department of Environmental Biotechnology, School of Environmental Sciences, Bharathidasan University, Tiruchirappalli, India",{"title":413},{"VI":414},"Umamaheswari Sundaresan",{"id":416,"sortIndex":21,"researcher":20,"roles":417,"affiliations":418,"properties":424},"8a8a931f-8346-4be3-af3d-f9f2e8672fd4",[162],[419],{"id":20,"sortIndex":21,"affiliation":420,"properties":20},{"id":406,"createTime":407,"updateTime":407,"relativeEntities":421,"slug":20,"properties":422,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":423},{"VI":411},{"title":425},{"VI":426},"Velusamy Arumugam",{"id":428,"sortIndex":429,"researcher":20,"roles":430,"affiliations":431,"properties":440},"f7f23ee9-3564-4b3c-8f3f-8ef61e28ede2",4,[162],[432],{"id":20,"sortIndex":21,"affiliation":433,"properties":20},{"id":434,"createTime":435,"updateTime":435,"relativeEntities":436,"slug":20,"properties":437,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"26511e6f-5069-4a43-90b0-b0791de428a5","2023-12-23T13:18:45.108+00:00",[],{"title":438},{"VI":439},"Department of Zoology, School of Natural Science, Ryan Institute, National University of Ireland, Galway, Ireland",{"title":441},{"VI":442},"Satheesh Kumar Palanisamy",{"id":444,"sortIndex":177,"researcher":20,"roles":445,"affiliations":446,"properties":465},"54ccd211-ff92-4b8d-8810-4b5c724e1516",[162],[447,455],{"id":20,"sortIndex":21,"affiliation":448,"properties":20},{"id":449,"createTime":450,"updateTime":450,"relativeEntities":451,"slug":20,"properties":452,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"32bfac98-0f24-48bc-80cd-62bf402119a6","2023-12-23T13:18:45.073+00:00",[],{"title":453},{"VI":454},"Department of Medical Biotechnology, Native Medicine and Marine Pharmacology Laboratory, Chettinad Academy of Research and Education, Chennai, India",{"id":456,"sortIndex":131,"affiliation":457,"properties":464},"69d0221c-1e70-413a-b017-ba0f7faf5ff6",{"id":458,"createTime":459,"updateTime":459,"relativeEntities":460,"slug":20,"properties":461,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"2e721204-0f47-479f-a486-2159f9f4c13f","2023-12-23T13:18:45.088+00:00",[],{"title":462},{"VI":463},"Department of Medicine, University of Texas Health Sciences Center San Antonio, San Antonio, USA",{},{"title":466},{"VI":467},"Karthik 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B, Bar-Or A (2012) Treatment of multiple sclerosis with anti-CD20 antibodies. 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Biophys J 101(10):2525–2534\nYang J, Roy A, Zhang Y (2013) Protein–ligand binding site recognition using complementary binding-specific substructure comparison and sequence profile alignment. Bioinformatics 29(20):2588–2595\nYu CS, Chen YC, Lu CH, Hwang JK (2006) Prediction of protein subcellular localization. Proteins 64(3):643–651\nYu C-S, Cheng C-W, Su W-C, Chang K-C, Huang S-W, Hwang J-K, Lu C-H (2014) CELLO2GO: a web server for protein subCELlular LOcalization prediction with functional gene ontology annotation. PLoS ONE 9(6):e99368\nZhang B (2009). Ofatumumab. MAbs, Taylor & Francis, Routledge",{"EN":539},"CD20 has been known as an attractive therapeutic target for refractory diseases such as B-cell chronic lymphocytic leukemia, rheumatoid arthritis and multiple sclerosis. Determining the 3D structure of the CD20 antigen could help to achieve a better deduction of its functions and its interactions with ligands. In this regard, we have launched an in silico protein modeling strategy to unveil the probable 3D structure of CD20 molecule. Various protein modeling approaches including homology modeling, Fold recognition and ab initio method were employed to build a qualified mode Protein BLAST tool from NCBI database was used to find a suitable template and the selected template was fed as input structure of the modeling software. Thereafter, the quality of the obtained models was evaluated invoking the model quality assessment software. CD20 Topology prediction shows that 4 trans membrane helixes. The best model predicted by LOMETS was selected for analyses. Refinement of 3D structure as well as determination of its B-cell epitopes, clefts and ligand binding sites was carried out on the structure. In conclusion, CD20 antigen 3D prediction led to design and production of a new monoclonal antibody.",{"EN":541},"In Silico Analysis for Determination and Validation of Human CD20 Antigen 3D Structure",{"VOID":543},"10.1007\u002Fs10989-017-9654-9","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10989-017-9654-9",[546,561,588,610],{"id":547,"sortIndex":482,"researcher":20,"roles":548,"affiliations":549,"properties":558},"2eab4318-a540-494d-ba2c-7cf42f9aa780",[162],[550],{"id":20,"sortIndex":21,"affiliation":551,"properties":20},{"id":552,"createTime":553,"updateTime":553,"relativeEntities":554,"slug":20,"properties":555,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"26d8698b-f907-4575-8e74-ac827f301098","2024-02-08T05:04:30.305+00:00",[],{"title":556},{"VI":557},"School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, 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Iran",{},{"id":20,"sortIndex":21,"affiliation":576,"properties":20},{"id":577,"createTime":578,"updateTime":579,"relativeEntities":580,"slug":581,"properties":582,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"7b4e8acf-e284-49d2-b76c-a24c2a13755d","2024-01-17T16:24:47.460+00:00","2024-12-18T10:08:12.492+00:00",[],"Department-of-Medical-Biotechnology-and-Nanotechnology-Faculty-of-Medicine-Zanjan-University-of-Medical-Sciences-Zanjan-Iran",{"title":583},{"VI":584},"Department of Medical Biotechnology and Nanotechnology, Faculty of Medicine, Zanjan University of Medical Sciences, Zanjan, Iran",{"title":586},{"VI":587},"Yousef Mortazavi",{"id":589,"sortIndex":131,"researcher":20,"roles":590,"affiliations":591,"properties":607},"f9568dfa-ee3c-41ee-9a64-65fa3118383b",[162],[592,599],{"id":593,"sortIndex":131,"affiliation":594,"properties":598},"3d2796e3-e536-4bb1-a8c7-55a9d1d8fb63",{"id":552,"createTime":553,"updateTime":553,"relativeEntities":595,"slug":20,"properties":596,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":597},{"VI":557},{},{"id":20,"sortIndex":21,"affiliation":600,"properties":20},{"id":601,"createTime":602,"updateTime":602,"relativeEntities":603,"slug":20,"properties":604,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"8f5263f6-695c-4752-9139-5b1d49ffb179","2024-01-10T15:02:03.780+00:00",[],{"title":605},{"VI":606},"Department of Clinical Biochemistry, Faculty of Medicine, Shahid Beheshti University of 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D. 1991 J. Org. Chem. 56:1713–1718\nXia M., Wang Y. G. 2002 Tetrahedron. Lett. 43:7703–7705",{"EN":1292},"As part of our efforts to design constrained peptide mimics and introduce them in peptide sequences, we set up the synthesis of racemic N-Fmoc protected hydroxypyrrolidine by reduction of the corresponding oxopyrroline. Hydroxypyrrolidines are synthesized using amino acid building block and β-ketoester via a 4-steps solid supported route on Wang resin beads. The hydroxypyrrolidine template can be seen as a constrained mimic of statine. As proof of concept, the pseudopeptide JMV 2776, incorporating this new statine mimic has been synthesized. We replaced the phenyl statine building block in the sequence of known BACE 1\u002F2 inhibitors by 5-benzyl 2-methyl 4-hydroxypyrrolidine, using conventional Fmoc SPPS on Rink amide PS resin.",{"EN":1294},"Solid Phase Synthesis of a Hydroxypyrrolidine Derivative and its Use in Solid Phase Peptide Synthesis as Constrained Statine 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citation_doi=10.1007\u002Fs10989-019-09869-5; citation_id=CR42\ncitation_journal_title=J Food Sci; citation_title=Antioxidant peptide fractions isolated from wheat germ protein with subcritical water extraction and its transport across Caco2 cells; citation_author=J Zhang, C Wen, C Li, Y Duan, H Zhang, H Ma; citation_volume=84; citation_issue=8; citation_publication_date=2019; citation_pages=2139-2146; citation_id=CR43\ncitation_journal_title=Process Biochem; citation_title=Antioxidant and free radicalscavenging activities of wheat germ protein hydrolysates (WGPH) prepared with alcalase; citation_author=KX Zhu, HM Zhou, H Qian; citation_volume=41; citation_publication_date=2006; citation_pages=1296-1302; citation_id=CR44",{"EN":1408,"VI":1409},"In this study, the effect of wheat germ protein hydrolysates (WGPH) on physicochemical and sensory properties of frozen yogurt was investigated. For this purpose, first, the WGPH was produced using two enzymes, alcalase and flavourzyme, and its functional properties were determined to find the best enzyme, and then 4 treatments of frozen yogurt, containing 0, 0.5, 1 and 1.5% of the WGPH was prepared and the physicochemical and sensory properties of frozen yogurt were investigated. The results related to the properties of WGPH showed that among the enzymes, alcalase can produce a WGPH with a higher degree of hydrolysis, solubility, foaming, and emulsion properties, Thus the WGPH by the alcalase enzyme was added to the frozen yogurt. The results related to the properties of frozen yogurt showed that the samples with WGPH had a higher pH, viscosity, uranium, melting resistance, and texture hardness than the control and better results were observed by increasing concentration of WGPH, but WGPH at 1.5% was not approved by the evaluators. Although no specific international standard has been codified for frozen yogurt, according to the results, WGPH at 1% is recommended as the best treatment that can be provided to consumers as a new, high quality, and marketable product.","Trong nghiên cứu này, tác động của protein thủy phân từ mầm lúa mì (WGPH) lên các đặc tính vật lý - hóa học và cảm quan của sữa chua đông lạnh đã được điều tra. Để thực hiện điều này, trước tiên, WGPH được sản xuất bằng cách sử dụng hai enzyme, alcalase và flavourzyme, và các đặc tính chức năng của nó đã được xác định để tìm ra enzyme tối ưu. Sau đó, 4 loại sữa chua đông lạnh được chuẩn bị, bao gồm 0, 0.5, 1 và 1.5% WGPH, và các đặc tính vật lý - hóa học cũng như cảm quan của sữa chua đông lạnh đã được nghiên cứu. Kết quả liên quan đến các đặc tính của WGPH cho thấy, trong số các enzyme, alcalase có khả năng tạo ra WGPH với mức độ thủy phân, độ tan, tính tạo bọt và tính nhũ tương cao hơn, vì vậy WGPH từ enzyme alcalase đã được thêm vào sữa chua đông lạnh. Kết quả liên quan đến các đặc tính của sữa chua đông lạnh cho thấy các mẫu có WGPH có pH, độ nhớt, độ urani, khả năng chống chảy và độ cứng về kết cấu cao hơn so với mẫu đối chứng, và kết quả tốt hơn được quan sát thấy khi tăng nồng độ WGPH, tuy nhiên WGPH ở nồng độ 1.5% không được các nhà đánh giá chấp nhận. Mặc dù chưa có tiêu chuẩn quốc tế cụ thể nào được xác định cho sữa chua đông lạnh, theo kết quả, WGPH ở nồng độ 1% được khuyến nghị là phương pháp điều trị tốt nhất có thể cung cấp cho người tiêu dùng như một sản phẩm mới, chất lượng cao và có khả năng thị trường.",{"EN":1411,"VI":1412},"Evaluation of Functional Properties of Wheat Germ Protein Hydrolysates and Its Effect on Physicochemical Properties of Frozen Yogurt","Đánh giá các đặc tính chức năng của protein thủy phân từ mầm lúa mì và tác động của nó đến các đặc tính vật lý - hóa học của sữa chua đông lạnh",{"VOID":1414},"10.1007\u002Fs10989-022-10378-1",{"VI":1416},"WGPH, protein thủy phân, mầm lúa mì, sữa chua đông lạnh, đặc tính vật lý - hóa học, enzyme alcalase, cảm quan","2025-02-05T18:34:21.732+00:00",[1419],"VI","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10989-022-10378-1","https:\u002F\u002Flink.springer.com\u002Fcontent\u002Fpdf\u002F10.1007\u002Fs10989-022-10378-1.pdf",[1423,1438,1450],{"id":1424,"sortIndex":21,"researcher":20,"roles":1425,"affiliations":1426,"properties":1435},"fe1b04b3-9b06-452b-9af3-ed9efe051ec9",[162],[1427],{"id":20,"sortIndex":21,"affiliation":1428,"properties":20},{"id":1429,"createTime":1430,"updateTime":1430,"relativeEntities":1431,"slug":20,"properties":1432,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"31019f5c-3bfe-491d-8d3a-3123d95a99d7","2024-01-28T12:17:47.846+00:00",[],{"title":1433},{"VI":1434},"Department of Food Science and Technology, Ayatolla Amoli Branch, Islamic Azad University, Amol, Iran",{"title":1436},{"VI":1437},"Ghelich, Sekineh",{"id":1439,"sortIndex":177,"researcher":20,"roles":1440,"affiliations":1441,"properties":1447},"03f8ca96-0c1e-4914-8440-dcf5ec387a17",[162],[1442],{"id":20,"sortIndex":21,"affiliation":1443,"properties":20},{"id":1429,"createTime":1430,"updateTime":1430,"relativeEntities":1444,"slug":20,"properties":1445,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1446},{"VI":1434},{"title":1448},{"VI":1449},"Ahmadi, Mohammad",{"id":1451,"sortIndex":131,"researcher":20,"roles":1452,"affiliations":1453,"properties":1459},"f0796b04-1a5e-4c24-bd37-11245e6521c3",[162],[1454],{"id":20,"sortIndex":21,"affiliation":1455,"properties":20},{"id":1429,"createTime":1430,"updateTime":1430,"relativeEntities":1456,"slug":20,"properties":1457,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1458},{"VI":1434},{"title":1460},{"VI":1461},"Ariaii, Peiman",{"url":1420,"publisher":1463,"properties":1491},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1464,"slug":10,"properties":1465,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1469,"manageAffiliations":1470,"indexDatabases":1471,"url":20,"thumbnailPath":20,"statistic":1486,"gsStatistic":20,"type":20,"analyzePriority":20},[],{"issn":1466,"eissn":1467,"title":1468},{"VOID":13},{"VOID":15},{"EN":17},[],[],[1472,1479],{"id":88,"indexDatabase":1473,"url":103,"indexYears":20,"academicFieldIds":1478,"indexDatabaseRanking":20},{"id":90,"createTime":91,"updateTime":92,"relativeEntities":1474,"label":1475,"description":1476,"key":99,"publicationTags":1477,"standard":20},[],{"EN":95,"VI":95},{"VI":97,"EN":98},[101,102],[105],{"id":107,"indexDatabase":1480,"url":120,"indexYears":121,"academicFieldIds":1485,"indexDatabaseRanking":128},{"id":109,"createTime":110,"updateTime":111,"relativeEntities":1481,"label":1482,"description":1483,"key":117,"publicationTags":1484,"standard":20},[],{"EN":114,"VI":114},{"EN":114,"VI":116},[119],[123,124,125,126,127],{"impactFactor":21,"impactFactorByYear":1487,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":131,"totalPublicationByYear":1488,"totalCitation":21,"totalCitationByYear":1489,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":1490,"hindexLast5Year":21,"hindex":21},{},{"2020":131},{},{},{"volume":1492,"pages":1494,"issue":1496},{"VOID":1493},"28",{"VOID":1495},"1-12",{"VOID":1497},"2","2022-03-01",2022,{"id":1501,"createTime":1502,"updateTime":1503,"relativeEntities":1504,"slug":1505,"properties":1506,"entityType":154,"verifyStatus":155,"verifyTime":1503,"verifyNote":156,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1515,"fullTextUrl":20,"authors":1516,"publicationType":203,"publisherRelationship":1571,"citationCount":20,"citationInfo":20,"publishDate":1605,"publishYear":1606,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":20,"openAccess":20,"references":20,"isForceReanalyzing":240},"60572589-1419-4656-acc6-106dc3f712c2","2023-12-19T15:12:23.024+00:00","2025-02-12T23:47:49.713+00:00",[],"A-12-Crown-4-Ether-Containing-Dipeptide-Boc-12-Crown-4-l-DOPA-Gly-OMe-Induces-Cell-Cycle-Arrest-and-Apoptosis-in-Rat-Eggs-Cultured-In-Vitro",{"references":1507,"abstract":1509,"title":1511,"doi":1513},{"VOID":1508},"Arenaz P, Bitticks L, Pannell K, Garcia S (1989) Genotoxic potential of crown ethers in Salmonella typhimurium. Mutagenesis 4:437–438\nArmarego WLF, Perrin DD (1997) Purification of laboratory chemicals, 4th edn. Butterworth-Heinemann, Oxford, pp 48–60\nBagshawe KD, Springer CJ, Searle F, Antoniw P, Sharma SK, Melton RG, Sherwood RF (1988) A cytotoxic agent can be generated selectively at cancer sites. Br J Cancer 58:700–703\nBoudreault PL, Voyer N (2007) Synthesis, characterization and cytolytic activity of alpha-helical amphiphilic peptide nanostructures containing crown ethers. Org Biomol Chem 5:1459–1465\nBoudreault PL, Arseneault M, Otis F, Voyer N (2008) Nanoscale tools to selectively destroy cancer cells. Chem Commun (Camb) 14:2118–2120\nBrandt K, Kruszynksi R, Bartczak TJ, Porwoli-Czomperlik I (2001) AIDS-related lymphoma screen results and molecular structure determination of a new crown ether bearing aziridinylcyclophosphazene, potentially capable of ion-regulated DNA cleavage action. Inorg Chem Acta 322:138–144\nCorvis Y, Korchowiec B, Korchowiec J, Badis M, Mironiuk-Puchalska E, Fokt I, Priebe W, Rogalska E (2008) Complexation of metal ions in langmuir films formed with two amphiphilic dioxadithia crown ethers. J Phys Chem B 112:10953–10963\nCotter TG (2009) Apoptosis and cancer: the genesis of a research field. Nat Rev Cancer 9:501–507\nCram DJ (1988) The design of molecular hosts, guests, and their complexes (Nobel Lecture). Angew Chem Int Ed Engl 27:1009–1020\nde Bruin EC, Medema JP (2008) Apoptosis and non-apoptotic deaths in cancer development and treatment response. Cancer Treat Rev 34:737–749\nGokel GW, Barbour LJ, Ferdani R, Hu J (2002) Lariat ether receptor systems show experimental evidence for alkali metal cation-pi interactions. Acc Chem Res 35:878–886\nGokel GW, Leevy WM, Weber ME (2004) Crown ethers: sensors for ions and molecular scaffolds for materials and biological models. Chem Rev 104:2723–2750\nGupta SK, Malik A, Arukha AP (2015) Ovarian and oocyte targets for development of female contraceptives. Expert OpinTher Targets. doi:10.1517\u002F14728222.2015.1051305\nHall AC, Suarez C, Hom-Choudhury A, Manu ANA, Hall CD, Kirkovits GJ, Ghiriviga I (2003) Cation transport by a redox-active synthetic ion channel. Org Biomol Chem 1:2973–2982\nHao Y, Lai L, Mao J, Im GS, Bonk A, Prather RS (2004) Apoptosis in parthenogenetic preimplantation porcine embryos. Biol Reprod 70:1644–1649\nJansen BAJ, Wielaard P, Dulk HD, Brouwer J, Reedijk J (2002) Oxa-aza crown ethers as ligands for mixed-ligand cisplatin derivatives and dinuclear platinum anticancer drugs. Eur J Inorg Chem 2002:2375–2379\nJurisicova A, Acton BM (2004) Deadly decisions: the role of genes regulating programmed cell death in human preimplantation embryo development. Reproduction 128:281–291\nKerr JF, Wyllie AH, Currie AR (1972) Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 26:239–257\nLehn JM (1988) Supramolecular chemistry-scope and perspectives molecules, supermolecules, and molecular devices (Nobel Lecture). Angew Chem Int Ed Engl 27:89–112\nLu Q, Chen ZJ, Gao X, Ma SY, Li M, Hu JM, Li Y (2006) Oocyte activation with calcium ionophore A23187 and puromycin on human oocytes that failed to fertilize after intracytoplasmic sperm injection. Zhonghua Fu Chan KeZaZhi 41:182–185\nMarjanovic M, Kralj M, Supek F, Frkanec L, Piantanida I, Smuc T, Tusek-Bozic L (2007) Antitumor potential of crown ethers: structure-activity relationships, cell cycle disturbances, and cell death studies of a series of ionophores. J Med Chem 50:1007–1018\nMcPhee MM, Kern JT, Hoster BC, Kerwin SM (2000) Propargylic sulfone-armed lariat crown ethers: alkali metal ion-regulated DNA cleavage agents. Bioorg Chem 28:98–118\nMeillon JC, Voyer N (1997) A synthetic transmembrane channel active in lipid bilayers. Angew Chem Int Ed Engl 36:967–969\nPedersen CJ (1967) Cyclic polyethers and their complexes with metal salts. J Am Chem Soc 89:7017–7036\nPrasad S, Tiwari M, Tripathi A, Pandey AN, Chaube SK (2015) Changes in signal molecules and maturation promoting factor levels associate with spontaneous resumption of meiosis in rat oocytes. Cell Biol Int 39:759–769\nPremkumar KV, Chaube SK (2015) Nitric oxide signals postovulatory aging-induced abortive spontaneous egg activation in rats. Redox Rep 20:184–192\nRamalho-Santos J, Varum S, Amaral S, Mota PC, Sousa AP, Amaral A (2009) Mitochondrial functionality in reproduction: from gonads and gametes to embryos and embryonic stem cells. Hum Reprod Update 15:553–572\nRotello VM (2008) Crown ether-peptide construct selectively kills cancer cells. Chem Biol Drug Des 72:1–2\nRyoo HD, Bergmann A (2012) The Role of Apoptosis-induced proliferation for regeneration and cancer. Cold Spring Harb Perspect Biol 4:1–17\nTripathi A, Chaube SK (2012) High cytosolic free calcium level signals apoptosis through mitochondria-caspase mediated pathway in rat eggs cultured in vitro. Apoptosis 17:439–448\nTripathi A, Chaube SK (2015a) Reduction of phosphorylated Thr-161 Cdk1 level participates in roscovitine-induced Fas ligand-mediated apoptosis in rat eggs cultured in vitro. In Vitro Cell Dev Biol Anim 51:174–182\nTripathi A, Chaube SK (2015b) Roscovitine inhibits extrusion of second polar body and induces apoptosis in rat eggs cultured in vitro. Pharmacol Rep. doi:10.1016\u002Fj.pharep.2015.01.011\nTripathi G, Gurunath R (2015) Structures and conformation of a benzo-12-crown-4 containing dipeptide biopolymers. PeptSci 104:148–155\nTripathi A, Shrivastav TG, Chaube SK (2012) Aqueous extract of Azadirachta indica (neem) leaf induces generation of reactive oxygen species and mitochondria-mediated apoptosis in rat oocytes. J Assist Reprod Genet 29:15–23\nTripathi A, Shrivastav TG, Chaube SK (2013) An increase of granulosa cell apoptosis mediates aqueous neem (Azadirachta indica) leaf extract-induced oocyte apoptosis in rat. Int J Appl Basic Med Res 3:27–36\nTso WW, Fung WP, Tso MYW (1981) Variability of crown ether toxicity. J Inorg Biochem 14:237–244\nVandenburg YR, Smith BD, Biron E, Voyer N (2002) Membrane disruption ability of facially amphiphilic helical peptides. Chem Commun 21:1694–1695\nZhang X, Li XH, Ma X, Wang ZH, Lu S, Guo YL (2006) Redoxinduced apoptosis of human oocytes in resting follicles in vitro. J Soc Gynecol Investig 13:451–458",{"EN":1510},"The study was designed to investigate whether crown ether containing dipeptide Boc-12-crown-4-l-DOPA-Gly-OMe has potential to induce meiotic cell cycle arrest and apoptosis in rat eggs cultured in vitro. The immature female rats were subjected to superovulation induction protocol and ovulated eggs were collected from ampulla of the fallopian tube. Ovulated eggs arrested at metaphase-II (M-II) stage of meiotic cell cycle were cultured in media-199 with or without various concentrations (0.0, 0.025, 0.050, 0.10, and 0.20 mM) of dipeptide for 3 h in vitro. Morphological apoptotic changes, hydrogen peroxide (H2O2) concentration, cytochrome c level, caspase-3 level as well as activity and DNA fragmentation were analysed in eggs cultured in vitro. Culture of M-II arrested eggs in plain medium for 3 h in vitro induced meiotic exit from M-II arrest in majority of eggs as evidenced by initiation of extrusion of second polar body (II PB). The dipeptide induced maintenance of M-II arrest and morphological apoptotic features in a concentration-dependent manner prior to degeneration. The dipeptide-induced morphological features were associated with increased H2O2 and cytochrome c levels in treated eggs. The increased cytochrome c induced caspase-3 level and activity and thereby DNA fragmentation as evidenced by DAB positive staining in treated eggs. Our results suggest that dipeptide Boc-12-C-4-l-DOPA-Gly-OMe induces cell cycle arrest at M-II stage and apoptosis in rat eggs cultured in vitro.",{"EN":1512},"A 12-Crown-4 Ether Containing Dipeptide Boc-12-Crown-4-l-DOPA-Gly-OMe Induces Cell Cycle Arrest and Apoptosis in Rat Eggs Cultured In Vitro",{"VOID":1514},"10.1007\u002Fs10989-015-9484-6","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10989-015-9484-6",[1517,1532,1547,1559],{"id":1518,"sortIndex":21,"researcher":20,"roles":1519,"affiliations":1520,"properties":1529},"42baf393-bb37-4f7f-8dd7-53e65541f5ea",[162],[1521],{"id":20,"sortIndex":21,"affiliation":1522,"properties":20},{"id":1523,"createTime":1524,"updateTime":1524,"relativeEntities":1525,"slug":20,"properties":1526,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"18e6f725-3721-40ec-89f6-d159fa2c6c67","2024-01-28T04:57:25.173+00:00",[],{"title":1527},{"VI":1528},"Department of Chemistry, Indian Institute of Technology Kanpur, Kanpur, India",{"title":1530},{"VI":1531},"Garima Tripathi",{"id":1533,"sortIndex":482,"researcher":20,"roles":1534,"affiliations":1535,"properties":1544},"6afa8a61-02d5-40c7-9198-4eef46c2be79",[162],[1536],{"id":20,"sortIndex":21,"affiliation":1537,"properties":20},{"id":1538,"createTime":1539,"updateTime":1539,"relativeEntities":1540,"slug":20,"properties":1541,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},"c6537b5b-2b78-4054-b96b-fda9d3fd2a73","2023-12-20T15:09:06.227+00:00",[],{"title":1542},{"VI":1543},"Cell Physiology Laboratory, Biochemistry Unit, Department of Zoology, Banaras Hindu University, Varanasi, India",{"title":1545},{"VI":1546},"Shail K. Chaube",{"id":1548,"sortIndex":131,"researcher":20,"roles":1549,"affiliations":1550,"properties":1556},"4dc6f735-95b3-422f-b3f4-67096410c247",[162],[1551],{"id":20,"sortIndex":21,"affiliation":1552,"properties":20},{"id":1538,"createTime":1539,"updateTime":1539,"relativeEntities":1553,"slug":20,"properties":1554,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1555},{"VI":1543},{"title":1557},{"VI":1558},"Anima Tripathi",{"id":1560,"sortIndex":177,"researcher":20,"roles":1561,"affiliations":1562,"properties":1568},"a0ea53b2-dce2-4d8a-adcf-5365741e2425",[162],[1563],{"id":20,"sortIndex":21,"affiliation":1564,"properties":20},{"id":1523,"createTime":1524,"updateTime":1524,"relativeEntities":1565,"slug":20,"properties":1566,"entityType":73,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21},[],{"title":1567},{"VI":1528},{"title":1569},{"VI":1570},"Gurunath Ramanathan",{"url":1515,"publisher":1572,"properties":1600},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1573,"slug":10,"properties":1574,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1578,"manageAffiliations":1579,"indexDatabases":1580,"url":20,"thumbnailPath":20,"statistic":1595,"gsStatistic":20,"type":20,"analyzePriority":20},[],{"issn":1575,"eissn":1576,"title":1577},{"VOID":13},{"VOID":15},{"EN":17},[],[],[1581,1588],{"id":88,"indexDatabase":1582,"url":103,"indexYears":20,"academicFieldIds":1587,"indexDatabaseRanking":20},{"id":90,"createTime":91,"updateTime":92,"relativeEntities":1583,"label":1584,"description":1585,"key":99,"publicationTags":1586,"standard":20},[],{"EN":95,"VI":95},{"VI":97,"EN":98},[101,102],[105],{"id":107,"indexDatabase":1589,"url":120,"indexYears":121,"academicFieldIds":1594,"indexDatabaseRanking":128},{"id":109,"createTime":110,"updateTime":111,"relativeEntities":1590,"label":1591,"description":1592,"key":117,"publicationTags":1593,"standard":20},[],{"EN":114,"VI":114},{"EN":114,"VI":116},[119],[123,124,125,126,127],{"impactFactor":21,"impactFactorByYear":1596,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":131,"totalPublicationByYear":1597,"totalCitation":21,"totalCitationByYear":1598,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":1599,"hindexLast5Year":21,"hindex":21},{},{"2020":131},{},{},{"volume":1601,"pages":1603},{"VOID":1602},"22",{"VOID":1604},"57-66","2015-08-14",2015,{"id":1608,"createTime":1609,"updateTime":1610,"relativeEntities":1611,"slug":1612,"properties":1613,"entityType":154,"verifyStatus":155,"verifyTime":1610,"verifyNote":156,"syncStatus":19,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1622,"fullTextUrl":20,"authors":1623,"publicationType":203,"publisherRelationship":1675,"citationCount":20,"citationInfo":20,"publishDate":1709,"publishYear":1710,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":20,"openAccess":20,"references":20,"isForceReanalyzing":240},"39604ea5-8c4e-43c0-91ed-9721ff73f1a4","2024-01-05T03:03:39.234+00:00","2024-12-29T23:46:38.531+00:00",[],"Variants-of-Lipopeptides-Produced-by-Bacillus-licheniformis-HSN221-in-Different-Medium-Components-Evaluated-by-a-Rapid-Method-ESI-MS",{"references":1614,"abstract":1616,"title":1618,"doi":1620},{"VOID":1615},"Akpa E, Jacques P, Wathelet B et al (2001) Influence of culture conditions on lipopeptide production by Bacillus subtilis. Appl Biochem Biotechnol 91–93:551–561\nBonmatin JM, Laprévote O, Peypoux F (2003) Diversity among microbial cyclic lipopeptides: iturins and surfactins, activity-structure relationships to design new bioactive agents. Comb Chem High Throughput Screen 6:541–556\nCooper DG, Macdonald CR, Duff SJB et al (1981) Enhanced production of surfactin from Bacillus subtilis by continuous product removal and metal cation additions. Appl Environ Microbiol 42:408–412\nFox SL, Bala GA (2000) Production of surfactant from Bacillus subtilis ATCC 21332 using potato substrates. Bioresour Technol 75:235–240\nGrangemard I, Peypoux F, Wallach J et al (1997) Lipopeptides with improved properties: structure by NMR, purification by HPLC and structure-activity relationships of new isoleucyl-rich surfactins. J Pept Sci 3:145–154\nGrangemard I, Bonmatin JM, Bernillon J et al (1999) Lichenysin G, a novel family of lipopeptide biosurfactants from Bacillus licheniformis IM 1307: production, isolation and structural evaluation by NMR and mass spectrometry. J Antibiot 52:363–373\nGrangemard I, Wallach J, Maget-Dana R et al (2001) Lichenysin a more efficient cation chelator than surfactin. Appl Biochem Biotechnol 90:199–210\nHasumi K, Takizawa K, Takahashi F et al (1995) Inhibition of acyl-coA: cholesterol acyltransferase by isohalobacillin, a complex of novel cyclic acylpeptides produced by Bacillus sp. A1238. J Antibiot 48:1419–1424\nJiraporn T, Niran R, Takayuki K et al (2003) Production and characterization of biosurfactants from Bacillus licheniformis F2.2. Biosci Biotech Biochem 67(6):1239–1244\nKonz D, Doekel S, Marahiel AM (1999) Molecular and biochemical characterization of the protein template controlling biosynthesis of the lipopeptide lichenysin. J Bacteriol 181:133–140\nKowall M, Vater J, Kluge B et al (1998) Separation and characterization of surfactin isoforms produced by Bacillus subtilis OKB 105. J Colloid Interf Sci 204:1–8\nLeenders F, Stein TH, Kablitz B et al (1999) Rapid typing of Bacillus subtilis strains by their secondary metabolites using matrix-assisted laser desorption\u002Fionization mass spectrometry of intact cells. Rapid Commun Mass Spectrom 13:943–949\nLin SC, Minton MA, Sharma MM et al (1994) Structural and immunological characterization of a biosurfactant produced by Bacillus licheniformis JF-2. Appl Environ Microbiol 60:31–38\nLiu XY, Namir IAH, Yang SZ et al (2007) Structural characterization of eight cyclic lipopeptides produced by Bacillus subtilis HSO121. Protein Pept Lett 14(8):766–773\nMakkar RS, Cameotra SS (1997) Utilization of molasses for biosurfactant production by two Bacillus strains at thermophilic conditions. J Am Oil Chem Soc 74:887–889\nMakkar RS, Cameotra SS (1999) Biosurfactant production by microorganisms on unconventional carbon sources. J Surfactants Deterg 2(2):237–241\nMakkar RS, Cameotra SS (2002) Effects of various nutritional supplements on biosurfactant production by a strain of Bacillus subtilis at 45°C. J Surfactants Deterg 5(1):11–17\nNamir IAH, Liu XY, Yang SZ et al (2008) Surfactin isoforms from Bacillus subtilis HSO121: separation and characterization. Protein Pept Lett 15:265–269\nPeypoux F, Bonmatin JM, Wallach J (1999) Recent trends in the biochemistry of surfactin. Appl Microbiol Biotechnol 51(5):553–563\nTrischman JA, Jensen PR, Fenical W (1994) Halobacillin: a cyclic acylpeptide of the iturin class produced by a marine Bacillus. Tetrahedron Lett 35:5571–5574\nVater J, Gao XW, Hitzeroth G et al (2003) “Whole cell”—matrix-assisted laser desorption ionization-time of flight-mass spectrometry, an emerging technique for efficient screening of biocombinatorial libraries of natural compounds—present state of research. Comb Chem High Throughput Screen 6:557–567\nWang J, Liu J, Wang X et al (2004) Application of electrospray ionization mass spectrometry in rapid typing of fengycin homologues produced by Bacillus subtilis. Lett Appl Microbiol 39:98–102\nWei YH, Chu IM (1998) Enhancement of surfactin production in iron-enriched media by Bacillus subtilis ATCC 21332. Enzyme Microb Technol 22:724–728\nWei YH, Chu IM (2002) Mn2+ improves surfactin production by Bacillus subtilis. Biotechnol Lett 24:479–482\nYakimov MM, Timmis KN, Wray V et al (1995) Characterization of a new lipopeptides surfactant produced by thermotolerant and halotolerant subsurface Bacillus licheniformis BAS50. Appl Environ Microbiol 61(5):1706–1713\nYakimov MM, Fredrickson HL, Timmis KN (1996) Effect of heterogeneity of hydrophobic moieties on surface activity of lichenysin A, a lipopeptide biosurfactant from Bacillus licheniformis BAS50. Biotechnol Appl Biochem 23:13–18\nYakimov MM, Abraham WR, Meyer H et al (1999) Structure characterization of lichenysin A components by fast atom bombardment tandem mass spectrometry. Biochim Biophys Acta 1438:273–280\nYang SZ, Wei DZ, Mu BZ (2006) Determination of the amino acid sequence in a cyclic lipopeptide using MS with DHT mechanism. J Biochem Biophys Methods 68(1):69–74",{"EN":1617},"A lipopeptide producing strain was isolated from an oil field and identified as Bacillus licheniformis HSN221. Nine different substrates were used to cultivate the strain under the same incubation conditions. Using a rapid method, Electrospray Ionization Mass Spectrometry (ESI-MS) combined with Thin Layer Chromatography (TLC), nine different lipopeptide homologues were found and identified. The strain produced four [Leu]surfactin homologues, surfactin C13, surfactin C14, surfactin C15 and surfactin C16, when cultivated in the medium with glucose, yeast extract and ammonium chloride, but it produced five lichenysin homologues, lichenysin C12, lichenysin C13, lichenysin C14, lichenysin C15 and lichenysin C16, when cultivated in the remaining eight media. 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