pH-responsive high stability polymeric nanoparticles for targeted delivery of anticancer therapeutics
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Chabner, B. A. & Roberts, T. G. Chemotherapy and the war on cancer. Nat. Rev. Cancer 5, 65–72 (2005).
Cheung-Ong, K., Giaever, G. & Nislow, C. DNA-damaging agents in cancer chemotherapy: serendipity and chemical biology. Chem. Biol. 20, 648–659 (2013).
Maeda, H. & Khatami, M. Analyses of repeated failures in cancer therapy for solid tumors: poor tumor-selective drug delivery, low therapeutic efficacy and unsustainable costs. Clin. Transl. Med. 7, 11 (2018).
Szakács, G., Paterson, J. K., Ludwig, J. A., Booth-Genthe, C. & Gottesman, M. M. Targeting multidrug resistance in cancer. Nat. Rev. Drug Discov. 5, 219–234 (2006).
Lage, H. An overview of cancer multidrug resistance: a still unsolved problem. Cell. Mol. Life Sci. 65, 3145 (2008).
Palanikumar, L., Choi, E. S., Cheon, J. Y., Joo, S. H. & Ryu, J.-H. Noncovalent polymer-gatekeeper in mesoporous silica nanoparticles as a targeted drug delivery platform. Adv. Funct. Mater. 25, 957–965 (2015).
Benyettou, F. et al. Synthesis of silver nanoparticles for the dual delivery of doxorubicin and alendronate to cancer cells. J. Mater. Chem. B 3, 7237–7245 (2015).
Kinoh, H. et al. Nanomedicines eradicating cancer stem-like cells in vivo by pH-triggered intracellular cooperative action of loaded drugs. ACS Nano 10, 5643–5655 (2016).
Zhang, Y. et al. Macrophage-membrane-coated nanoparticles for tumor-targeted chemotherapy. Nano Lett. 18, 1908–1915 (2018).
Sun, X. et al. The blood clearance kinetics and pathway of polymeric micelles in cancer drug delivery. ACS Nano 12, 6179–6192 (2018).
Nishiyama, N., Matsumura, Y. & Kataoka, K. Development of polymeric micelles for targeting intractable cancers. Cancer Sci. 107, 867–874 (2016).
Cho, H., Gao, J. & Kwon, G. S. PEG-b-PLA micelles and PLGA-b-PEG-b-PLGA sol–gels for drug delivery. J. Controlled Release 240, 191–201 (2016).
Nel, A. E. et al. Understanding biophysicochemical interactions at the nano–bio interface. Nat. Mater. 8, 543–557 (2009).
Liu, B. & Thayumanavan, S. Importance of evaluating dynamic encapsulation stability of amphiphilic assemblies in serum. Biomacromolecules 18, 4163–4170 (2017).
Shi, J., Kantoff, P. W., Wooster, R. & Farokhzad, O. C. Cancer nanomedicine: progress, challenges and opportunities. Nat. Rev. Cancer 17, 20–37 (2017).
Zhao, Y. et al. Augmenting drug–carrier compatibility improves tumour nanotherapy efficacy. Nat. Commun. 7, 11221 (2016).
Palanikumar, L. et al. Importance of encapsulation stability of nanocarriers with high drug loading capacity for increasing in vivo therapeutic efficacy. Biomacromolecules 19, 3030–3039 (2018).
Rosenblum, D., Joshi, N., Tao, W., Karp, J. M. & Peer, D. Progress and challenges towards targeted delivery of cancer therapeutics. Nat. Commun. 9, 1–12 (2018).
Peer, D. et al. Nanocarriers as an emerging platform for cancer therapy. Nat. Nanotechnol. 2, 751–760 (2007).
Bazak, R., Houri, M., El Achy, S., Kamel, S. & Refaat, T. Cancer active targeting by nanoparticles: a comprehensive review of literature. J. Cancer Res. Clin. Oncol. 141, 769–784 (2015).
Carril, M. et al. In situ detection of the protein corona in complex environments. Nat. Commun. 8, 1–5 (2017).
Oh, J. Y. et al. Cloaking nanoparticles with protein corona shield for targeted drug delivery. Nat. Commun. 9, 1–9 (2018).
Gilleron, J. et al. Image-based analysis of lipid nanoparticle–mediated siRNA delivery, intracellular trafficking and endosomal escape. Nat. Biotechnol. 31, 638–646 (2013).
Sahay, G. et al. Efficiency of siRNA delivery by lipid nanoparticles is limited by endocytic recycling. Nat. Biotechnol. 31, 653–658 (2013).
Nguyen, V. P., Alves, D. S., Scott, H. L., Davis, F. L. & Barrera, F. N. A novel soluble peptide with pH-responsive membrane insertion. Biochemistry 54, 6567–6575 (2015).
Nguyen, V. P. et al. Mechanistic insights into the pH-dependent membrane peptide ATRAM. J. Controlled Release 298, 142–153 (2019).
Nguyen, V. P., Dixson, A. C. & Barrera, F. N. The effect of phosphatidylserine on a ph-responsive peptide is defined by its noninserting end. Biophysical J. 117, 659–667 (2019).
Han, M. et al. Mitochondrial delivery of doxorubicin via triphenylphosphine modification for overcoming drug resistance in MDA-MB-435/DOX cells. Mol. Pharmaceutics 11, 2640–2649 (2014).
Dai, Q., Walkey, C. & Chan, W. C. W. Polyethylene glycol backfilling mitigates the negative impact of the protein corona on nanoparticle cell targeting. Angew. Chem. Int. Ed. 53, 5093–5096 (2014).
Makadia, H. K. & Siegel, S. J. Poly Lactic-co-Glycolic Acid (PLGA) as biodegradable controlled drug delivery carrier. Polymers 3, 1377–1397 (2011).
Han, F. Y., Thurecht, K. J., Whittaker, A. K. & Smith, M. T. Bioerodable PLGA-based microparticles for producing sustained-release drug formulations and strategies for improving drug loading. Front Pharm. 7, 185 (2016).
Elzoghby, A. O., Samy, W. M. & Elgindy, N. A. Albumin-based nanoparticles as potential controlled release drug delivery systems. J. Controlled Release 157, 168–182 (2012).
Langer, K. et al. Optimization of the preparation process for human serum albumin (HSA) nanoparticles. Int. J. Pharmaceutics 257, 169–180 (2003).
Jiwpanich, S., Ryu, J.-H., Bickerton, S. & Thayumanavan, S. Noncovalent encapsulation stabilities in supramolecular nanoassemblies. J. Am. Chem. Soc. 132, 10683–10685 (2010).
Yu, D., Zhang, Y., Zhou, X., Mao, Z. & Gao, C. Influence of surface coating of PLGA particles on the internalization and functions of human endothelial cells. Biomacromolecules 13, 3272–3282 (2012).
Moore, T. L. et al. Nanoparticle colloidal stability in cell culture media and impact on cellular interactions. Chem. Soc. Rev. 44, 6287–6305 (2015).
Schöttler, S. et al. Protein adsorption is required for stealth effect of poly(ethylene glycol)- and poly(phosphoester)-coated nanocarriers. Nat. Nanotechnol. 11, 372–377 (2016).
Treuel, L. et al. Impact of protein modification on the protein corona on nanoparticles and nanoparticle–cell interactions. ACS Nano 8, 503–513 (2014).
Sun, C. et al. Unfolding and refolding of bovine serum albumin induced by cetylpyridinium bromide. Biophysical J. 88, 3518–3524 (2005).
Wang, X. et al. Glutathione-triggered “off–on” release of anticancer drugs from dendrimer-encapsulated gold nanoparticles. J. Am. Chem. Soc. 135, 9805–9810 (2013).
Palanikumar, L. et al. Noncovalent surface locking of mesoporous silica nanoparticles for exceptionally high hydrophobic drug loading and enhanced colloidal stability. Biomacromolecules 16, 2701–2714 (2015).
Fennelly, C. & Amaravadi, R. K. in Lysosomes: Methods and Protocols (eds. Öllinger, K. & Appelqvist, H.) 293–308 (Springer New York, 2017).
Piao, S. & Amaravadi, R. K. Targeting the lysosome in cancer. Ann. N. Y. Acad. Sci. 1371, 45–54 (2016).
Palanikumar, L. et al. Spatiotemporally and sequentially-controlled drug release from polymer gatekeeper–hollow silica nanoparticles. Sci. Rep. 7, 46540 (2017).
Rezvantalab, S. et al. PLGA-based nanoparticles in cancer treatment. Front. Pharmacol. 9, 1260 (2018).
Liu, H.-N. et al. Mitochondrial targeted doxorubicin-triphenylphosphonium delivered by hyaluronic acid modified and pH responsive nanocarriers to breast tumor: in vitro and in vivo Studies. Mol. Pharm. 15, 882–891 (2018).
Yu, Y. et al. Benzene carboxylic acid derivatized graphene oxide nanosheets on natural zeolites as effective adsorbents for cationic dye removal. J. Hazard. Mater. 260, 330–338 (2013).
Deponte, M. Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes. Biochimica et. Biophysica Acta 1830, 3217–3266 (2013).
Bansal, A. & Simon, M. C. Glutathione metabolism in cancer progression and treatment resistance. J. Cell Biol. 217, 2291–2298 (2018).
Paka, G. D. & Ramassamy, C. Optimization of curcumin-loaded PEG-PLGA nanoparticles by GSH functionalization: investigation of the internalization pathway in neuronal cells. Mol. Pharmaceutics 14, 93–106 (2017).
Jahanban-Esfahlan, A. & Panahi-Azar, V. Interaction of glutathione with bovine serum albumin: Spectroscopy and molecular docking. Food Chem. 202, 426–431 (2016).
Persi, E. et al. Systems analysis of intracellular pH vulnerabilities for cancer therapy. Nat. Commun. 9, 1–11 (2018).
Cairns, R. A., Harris, I. S. & Mak, T. W. Regulation of cancer cell metabolism. Nat. Rev. Cancer 11, 85–95 (2011).
Wyatt, L. C. et al. Peptides of pHLIP family for targeted intracellular and extracellular delivery of cargo molecules to tumors. PNAS 115, E2811–E2818 (2018).
Kocbek, P., Obermajer, N., Cegnar, M., Kos, J. & Kristl, J. Targeting cancer cells using PLGA nanoparticles surface modified with monoclonal antibody. J. Controlled Release 120, 18–26 (2007).
Cammarata, C. R., Hughes, M. E. & Ofner, C. M. Carbodiimide induced cross-linking, ligand addition, and degradation in gelatin. Mol. Pharmaceutics 12, 783–793 (2015).
Acar, H., Ting, J. M., Srivastava, S., LaBelle, J. L. & Tirrell, M. V. Molecular engineering solutions for therapeutic peptide delivery. Chem. Soc. Rev. 46, 6553–6569 (2017).
Penchala, S. C. et al. A biomimetic approach for enhancing the in vivo half-life of peptides. Nat. Chem. Biol. 11, 793–798 (2015).
Zorzi, A., Middendorp, S. J., Wilbs, J., Deyle, K. & Heinis, C. Acylated heptapeptide binds albumin with high affinity and application as tag furnishes long-acting peptides. Nat. Commun. 8, 16092 (2017).
Bern, M., Sand, K. M. K., Nilsen, J., Sandlie, I. & Andersen, J. T. The role of albumin receptors in regulation of albumin homeostasis: implications for drug delivery. J. Controlled Release 211, 144–162 (2015).
van Witteloostuijn, S. B., Pedersen, S. L. & Jensen, K. J. Half-life extension of biopharmaceuticals using chemical methods: alternatives to PEGylation. ChemMedChem 11, 2474–2495 (2016).
Woldetsadik, A. D., Vogel, M. C., Rabeh, W. M. & Magzoub, M. Hexokinase II–derived cell-penetrating peptide targets mitochondria and triggers apoptosis in cancer cells. FASEB J. 31, 2168–2184 (2017).
Wang, L. H., Rothberg, K. G. & Anderson, R. G. Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation. J. Cell Biol. 123, 1107–1117 (1993).
Schnitzer, J. E., Oh, P., Pinney, E. & Allard, J. Filipin-sensitive caveolae-mediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules. J. Cell Biol. 127, 1217–1232 (1994).
West, M. A., Bretscher, M. S. & Watts, C. Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells. J. Cell Biol. 109, 2731–2739 (1989).
Mastrobattista, E. et al. Functional characterization of an endosome-disruptive peptide and its application in cytosolic delivery of immunoliposome-entrapped proteins. J. Biol. Chem. 277, 27135–27143 (2002).
Wolf, J. et al. pH-dependent membrane interactions of the histidine-rich cell-penetrating peptide LAH4-L1. Biophysical J. 113, 1290–1300 (2017).
Gelderblom, H., Verweij, J., Nooter, K. & Sparreboom, A. Cremophor EL: the drawbacks and advantages of vehicle selection for drug formulation. Eur. J. Cancer 37, 1590–1598 (2001).
Blanco, E., Shen, H. & Ferrari, M. Principles of nanoparticle design for overcoming biological barriers to drug delivery. Nat. Biotechnol. 33, 941–951 (2015).
Rattan, R. et al. Nanoparticle-macrophage interactions: a balance between clearance and cell-specific targeting. Bioorg. Medicinal Chem. 25, 4487–4496 (2017).
Chanput, W., Mes, J. J. & Wichers, H. J. THP-1 cell line: an in vitro cell model for immune modulation approach. Int. Immunopharmacol. 23, 37–45 (2014).
Meibohm, B. & Derendorf, H. Basic concepts of pharmacokinetic/pharmacodynamic (PK/PD) modelling. Int J. Clin. Pharm. Ther. 35, 401–413 (1997).
Majorek, K. A. et al. Structural and immunologic characterization of bovine, horse, and rabbit serum albumins. Mol. Immunol. 52, 174–182 (2012).
Sleep, D., Cameron, J. & Evans, L. R. Albumin as a versatile platform for drug half-life extension. Biochimica et. Biophysica Acta 1830, 5526–5534 (2013).
Tonigold, M. et al. Pre-adsorption of antibodies enables targeting of nanocarriers despite a biomolecular corona. Nat. Nanotech. 13, 862–869 (2018).
Smith, P. K. et al. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150, 76–85 (1985).
Nakamura, M., Kiyohara, S., Saito, K., Sugita, K. & Sugo, T. Chiral separation of DL-tryptophan using porous membranes containing multilayered bovine serum albumin crosslinked with glutaraldehyde. J. Chromatogr. A 822, 53–58 (1998).
Silva, C. S. P. C. O., Sousa, F. M. C., Guebitz, G. M. & Paulo, A. C. Chemical modifications on proteins using glutaraldehyde. Food Technol. Biotechnol. 42, 51–56 (2004).
Rajdev, P. & Ghosh, S. Fluorescence resonance energy transfer (FRET): a powerful tool for probing amphiphilic polymer aggregates and supramolecular polymers. J. Phys. Chem. B 123, 327–342 (2019).
Huang, W. et al. Surfactin-based nanoparticles loaded with doxorubicin to overcome multidrug resistance in cancers. Int. J. Nanomed. 13, 1723 (2018).
Ali, L. et al. The O-glycomap of lubricin, a novel mucin responsible for joint lubrication, identified by site-specific glycopeptide analysis. Mol. Cell. Proteom. 13, 3396–3409 (2014).
The UniProt Consortium. The universal protein resource (UniProt). Nucleic Acids Res. 36, D190–D195 (2008).
Tyanova, S., Temu, T. & Cox, J. The MaxQuant computational platform for mass spectrometry-based shotgun proteomics. Nat. Protoc. 11, 2301–2319 (2016).
Cox, J. et al. Andromeda: a peptide search engine integrated into the maxquant environment. J. Proteome Res. 10, 1794–1805 (2011).
He, S. et al. Quantitative and label-free detection of protein kinase A activity based on surface-enhanced raman spectroscopy with gold nanostars. Anal. Chem. 90, 6071–6080 (2018).
Schindelin, J. et al. Fiji: an open-source platform for biological-image analysis. Nat. Methods 9, 676–682 (2012).
Barltrop, J. A., Owen, T. C., Cory, A. H. & Cory, J. G. 5-(3-carboxymethoxyphenyl)-2-(4,5-dimethylthiazolyl)-3-(4-sulfophenyl)tetrazolium, inner salt (MTS) and related analogs of 3-(4,5-dimethylthiazolyl)-2,5-diphenyltetrazolium bromide (MTT) reducing to purple water-soluble formazans As cell-viability indicators. Bioorg. Medicinal Chem. Lett. 1, 611–614 (1991).
Berridge, M. V. & Tan, A. S. Characterization of the cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT): subcellular localization, substrate dependence, and involvement of mitochondrial electron transport in MTT reduction. Arch. Biochem. Biophysics 303, 474–482 (1993).
Koopman, G. et al. Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis. Blood 84, 1415–1420 (1994).
Tsarouchas, T. M. et al. Dynamic control of proinflammatory cytokines Il-1β and Tnf-α by macrophages in zebrafish spinal cord regeneration. Nat. Commun. 9, 1–17 (2018).
Meng, F. & Lowell, C. A. Lipopolysaccharide (LPS)-induced macrophage activation and signal transduction in the absence of Src-family kinases Hck, Fgr, and Lyn. J. Exp. Med. 185, 1661–1670 (1997).
National Research Council (US) Committee for the Update of the Guide for the Care and Use of Laboratory Animals. Guide for the Care and Use of Laboratory Animals. (National Academies Press (US), 2011).
Alhareth, K., Vauthier, C., Gueutin, C., Ponchel, G. & Moussa, F. HPLC quantification of doxorubicin in plasma and tissues of rats treated with doxorubicin loaded poly(alkylcyanoacrylate) nanoparticles. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 887–888, 128–132 (2012).
Bowerman, C. J. et al. Docetaxel-Loaded PLGA Nanoparticles Improve Efficacy in Taxane-Resistant Triple-Negative Breast Cancer. Nano Lett. 17, 242–248 (2017).