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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389013%3A_____%2F20%3A00522680" target="_blank" >RIV/61389013:_____/20:00522680 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216275:25310/19:39914952

Výsledek na webu

<a href="https://onlinelibrary.wiley.com/doi/full/10.1002/app.48725" target="_blank" >https://onlinelibrary.wiley.com/doi/full/10.1002/app.48725</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/app.48725" target="_blank" >10.1002/app.48725</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

20903 - Bioproducts (products that are manufactured using biological material as feedstock) biomaterials, bioplastics, biofuels, bioderived bulk and fine chemicals, bio-derived novel materials

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Applied Polymer Science

ISSN

0021-8995

e-ISSN

—

Svazek periodika

137

Číslo periodika v rámci svazku

21

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

1-10

Kód UT WoS článku

000496555800001

EID výsledku v databázi Scopus

2-s2.0-85075144046