Investigating the effect of food additive dye “tartrazine” on BLG fibrillation under in-vitro condition. A biophysical and molecular docking study
Tài liệu tham khảo
Abelein, 2013, Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates, J. Biol. Chem., 288, 23518, 10.1074/jbc.M113.470450
Adeniji, 2020, In silico study for evaluating the binding mode and interaction of 1,2,4-triazole and its derivatives as potent inhibitors against Lipoate protein B (LipB), J. King Saud Univ. – Sci., 32, 475, 10.1016/j.jksus.2018.07.014
Ali, 2019
Al-Shabib, 2017, Synthetic food additive dye “Tartrazine” triggers amorphous aggregation in cationic myoglobin, Int. J. Biol. Macromol., 98, 277, 10.1016/j.ijbiomac.2017.01.097
Arosio, 2015, On the lag phase in amyloid fibril formation, Phys. Chem. Chem. Phys., 17, 7606, 10.1039/C4CP05563B
Biancalana, 2010, Molecular mechanism of Thioflavin-T binding to amyloid fibrils, Biochim. Biophys. Acta, 1804, 1405, 10.1016/j.bbapap.2010.04.001
Bieler, 2005, Amyloid formation modulates the biological activity of a bacterial protein, J. Biol. Chem., 280, 26880, 10.1074/jbc.M502031200
Blancas-Mejía, 2013, Systemic amyloidoses, Annu. Rev. Biochem., 82, 745, 10.1146/annurev-biochem-072611-130030
Chiti, 2017, Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade, Annu. Rev. Biochem., 86, 27, 10.1146/annurev-biochem-061516-045115
Chiti, 1999, Designing conditions for in vitro formation of amyloid protofilaments and fibrils, Proc. Natl. Acad. Sci. USA, 96, 3590, 10.1073/pnas.96.7.3590
Collins, 1990, Study of the teratogenic potential of FD & C yellow No. 5 when given by gavage to rats, Food Chem. Toxicol., 28, 821, 10.1016/0278-6915(90)90055-R
Eman, 2000, Effects of some food colorants (synthetic and natural products) of young albino rats, Egypt. J. Hosp. Med., 1, 103, 10.21608/ejhm.2000.11021
Foderà, 2008, Secondary nucleation and accessible surface in insulin amyloid fibril formation, J. Phys. Chem. B, 112, 3853, 10.1021/jp710131u
Gottschalk, 2003, Protein self-association in solution: The bovine β -lactoglobulin dimer and octamer, Protein Sci., 12, 2404, 10.1110/ps.0305903
Grey, 2011, Membrane interaction of α-synuclein in different aggregation states, J. Parkinsons Dis., 1, 359, 10.3233/JPD-2011-11067
Hofer, 1997, Quick spectrophotometric identification of synthetic food colorants by linear regression analysis, Food Res. Technol., 204, 32
Ismael, 2018, Unraveling the molecular mechanism of the effects of sodium dodecyl sulfate, salts, and sugars on amyloid fibril formation in camel IgG, Colloids Surf. B Biointerfaces, 170, 430, 10.1016/j.colsurfb.2018.06.035
Khan, 2016, Cetyltrimethylammonium bromide (CTAB) promote amyloid fibril formation in carbohydrate binding protein (concanavalin A) at physiological pH, RSC Adv., 6, 38100, 10.1039/C6RA03707K
Khan, 2018, Sodium louroyl sarcosinate (sarkosyl) modulate amyloid fibril formation in hen egg white lysozyme (HEWL) at alkaline pH: a molecular insight study, J. Biomol. Struct. Dyn., 36, 1550, 10.1080/07391102.2017.1329097
Khan, 2016, The Achilles’ Heel of “Ultrastable” hyperthermophile proteins: submillimolar concentrations of SDS stimulate rapid conformational change, aggregation, and amyloid formation in proteins carrying overall positive charge, Biochemistry, 55, 3920, 10.1021/acs.biochem.5b01343
Khan, 2018, Cationic surfactant mediated fibrillogenesis in bovine liver catalase: a biophysical approach, J. Biomol. Struct. Dyn., 36, 2543, 10.1080/07391102.2017.1363085
Kong, 2017, Effects of seeding on lysozyme amyloid fibrillation in the presence of epigallocatechin and polyethylene glycol, Biochemistry (Mosc), 82, 156, 10.1134/S0006297917020079
Kumar, 2017, Kinetics of protein fibril formation: Methods and mechanisms, Int. J. Biol. Macromol., 100, 3, 10.1016/j.ijbiomac.2016.06.052
Kumar, 2014, Stages and conformations of the Tau repeat domain during aggregation and its effect on neuronal toxicity, J. Biol. Chem., 289, 20318, 10.1074/jbc.M114.554725
Liang, 2008, Interaction of beta-lactoglobulin with resveratrol and its biological implications, Biomacromolecules, 9, 50, 10.1021/bm700728k
Loch, 2011, Two modes of fatty acid binding to bovine beta-lactoglobulin-crystallographic and spectroscopic studies, J. Mol. Recognit., 24, 341, 10.1002/jmr.1084
Mecherfi, 2019, Combined microwave processing and enzymatic proteolysis of bovine whey proteins: the impact on bovine b-lactoglobulin allergenicity, J. Food Sci. Technol., 56, 177, 10.1007/s13197-018-3471-9
Merinas-Amo, 2019, Biological effects of food coloring in in vivo and in vitro model system, Foods, 8, 176, 10.3390/foods8050176
Michaels, 2015, Kinetic theory of protein filament growth: Self-consistent methods and perturbative techniques, Int. J. Mod. Phys. B, 29, 1530002, 10.1142/S0217979215300029
Morris, 2009, Autodock4 and AutoDockTools4: automated docking with selective receptor flexiblity, J. Comput. Chem., 16, 2785, 10.1002/jcc.21256
Ozawa, 2011, Inhibition of beta2-microglobulin amyloid fibril formation by alpha2-macroglobulin, J. Biol. Chem., 286, 9668, 10.1074/jbc.M110.167965
Poul, 2009, Lack of genotoxic effect of food dyes amaranth, sunset yellow and tartrazine and their metabolites in the gut micronucleus assay in mice, Food Chem. Toxicol., 47, 443, 10.1016/j.fct.2008.11.034
Rehman, 2016, Interaction of meropenem with ‘N’ and ‘B’ isoforms of human serum albumin: a spectroscopic and molecular docking study, J. Biomol. Struct. Dyn., 34, 1849, 10.1080/07391102.2015.1094411
Rizzuti, 2010, Native β-lactoglobulin self-assembles into a hexagonal columnar phase on a solid surface, Langmuir, 26, 1090, 10.1021/la902464f
Sahihi, 2012, The interaction of polyphenol flavonoids with β-lactoglobulin: molecular docking and molecular dynamics simulation studies, J. Macromol. Sci. B, 51, 2311, 10.1080/00222348.2012.672854
Schmitt, 2007, Whey protein soluble aggregates from heating with NaCl: physicochemical, interfacial, and foaming properties, Langmuir, 23, 4155, 10.1021/la0632575
Shicheng, 2017, Characterization of molecular structures of theaflavins and the interactions with bovine serum albumin, J. Food Sci. Technol. Mys., 54, 3421, 10.1007/s13197-017-2791-5
Shirahama, 1996, High resolution electron microscopic analysis of the amyloid fibril, J. Cell Biol., 33, 679, 10.1083/jcb.33.3.679
Tanaka, 2008, Effects of tartrazine on exploratory behavior in a three-generation toxicity study in mice, Reprod. Toxicol., 26, 156, 10.1016/j.reprotox.2008.07.001
Timasheff, 1964, Structure of the β-lactoglobulin tetramer, Nature, 203, 517, 10.1038/203517a0
Uhrinova, 2000, Structural changes accompanying pH-induced dissociation of the beta-lactoglobulin dimer, Biochemistry, 39, 3565, 10.1021/bi992629o
Verheul, 1999, Association behavior of native α-lactoglobulin, Biopolymers, 49, 11, 10.1002/(SICI)1097-0282(199901)49:1<11::AID-BIP2>3.0.CO;2-1
Wawer, 2018, Influence of the ionic strength on the amyloid fibrillogenesis of hen egg white lysozyme, Int. J. Biol. Macromol., 121, 63, 10.1016/j.ijbiomac.2018.09.165
Wetzel, 1987, Conformations of different gelatins in solutions and in films an analysis of circular dichroism (CD) measurements, Colloid Polym. Sci., 265, 1036, 10.1007/BF01417460