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Colloidally stable polypeptide‐based nanogel: study of enzyme‐mediated nanogelation in inverse miniemulsion

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    0522680 - ÚMCH 2021 RIV US eng J - Journal Article
    Dvořáková, Jana - Šálek, Petr - Korecká, L. - Pavlova, Ewa - Černoch, Peter - Janoušková, Olga - Koutníková, Barbora - Proks, Vladimír
    Colloidally stable polypeptide‐based nanogel: study of enzyme‐mediated nanogelation in inverse miniemulsion.
    Journal of Applied Polymer Science. Roč. 137, č. 21 (2020), s. 1-10, č. článku 48725. ISSN 0021-8995. E-ISSN 1097-4628
    R&D Projects: GA ČR(CZ) GA18-03224S
    Institutional support: RVO:61389013
    Keywords : biocompatible * biodegradable * human plasma
    OECD category: Bioproducts (products that are manufactured using biological material as feedstock) biomaterials, bioplastics, biofuels, bioderived bulk and fine chemicals, bio-derived novel materials
    Impact factor: 3.125, year: 2020
    Method of publishing: Limited access
    https://onlinelibrary.wiley.com/doi/full/10.1002/app.48725

    The current work presents a pivotal study of the nanogelation of the linear poly(N5‐2‐hydroxypropyl‐L‐glutamine) polymer precursor containing tyramine (TYR) units in an inverse miniemulsion by horseradish peroxidase/H2O2‐mediated crosslinking. The effects of various nH2O2/nTYR ratios on the kinetics of nanogelation in the inverse miniemulsion and on the reaction time are investigated by linear sweep voltammetry, while the formation of dityramine crosslinking is explored by fluorescence spectroscopy. The study is completed using dynamic light scattering measurements, nanoparticle tracking analysis, and cryogenic transmission electron microscopy to acquire comprehensive information about the formed nanoparticulate systems. With the optimal ratio nH2O2/nTYR = 2, the strategy yields in the high‐quality ~ 130 nm poly(amino acid)‐based nanogel, which is prepared in 2 h. The nanogel is colloidally stable under different temperature and pH conditions for over 168 h. Moreover, the demonstrated nanogel is noncytotoxic for HeLa cells and human primary fibroblasts and is quickly enzymatically hydrolyzed into small fragments during a biodegradation study in human blood plasma.
    Permanent Link: http://hdl.handle.net/11104/0312652

     
     
Number of the records: 1  

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