Enzymatic degradation of the hydrogels based on synthetic poly(.alpha.-amino acid)s

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389013%3A_____%2F11%3A00359220" target="_blank" >RIV/61389013:_____/11:00359220 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s10856-011-4275-x" target="_blank" >http://dx.doi.org/10.1007/s10856-011-4275-x</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s10856-011-4275-x" target="_blank" >10.1007/s10856-011-4275-x</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Enzymatic degradation of the hydrogels based on synthetic poly(.alpha.-amino acid)s

Popis výsledku v původním jazyce

Biodegradable hydrogels are studied as potential scaffolds for soft tissue regeneration. In this work biodegradable hydrogels were prepared from synthetic poly (a-amino acid)s, poly(AA)s. The covalently crosslinked gels were formed by radical copolymerization of methacryloylated poly(AA)s, e.g. poly[N5-(2-hydroxy-ethyl)-L-Glu- ran-L-Ala-ran-N6-methacryloyl-L-Lys], as a multifunctional macromer with a low-molecular-weight methacrylic monofunctional monomer, e.g. HEMA. Due to their polypeptide backbone, synthetic poly(AA)s are cleavable in biological environment by enzyme-catalyzed hydrolysis. The feasibility of enzymatic degradation of poly(AA)s alone and the hydrogels made from them was studied using elastase, a matrix proteinase involved in tissue healing processes, as a model enzyme. Specificity of elastase for cleavage of polypeptide chains behind the L-Ala residues was reflected in faster degradation of L-Ala-containing copolymers as well as of hydrogels composed of them.

Název v anglickém jazyce

Enzymatic degradation of the hydrogels based on synthetic poly(.alpha.-amino acid)s

Popis výsledku anglicky

Biodegradable hydrogels are studied as potential scaffolds for soft tissue regeneration. In this work biodegradable hydrogels were prepared from synthetic poly (a-amino acid)s, poly(AA)s. The covalently crosslinked gels were formed by radical copolymerization of methacryloylated poly(AA)s, e.g. poly[N5-(2-hydroxy-ethyl)-L-Glu- ran-L-Ala-ran-N6-methacryloyl-L-Lys], as a multifunctional macromer with a low-molecular-weight methacrylic monofunctional monomer, e.g. HEMA. Due to their polypeptide backbone, synthetic poly(AA)s are cleavable in biological environment by enzyme-catalyzed hydrolysis. The feasibility of enzymatic degradation of poly(AA)s alone and the hydrogels made from them was studied using elastase, a matrix proteinase involved in tissue healing processes, as a model enzyme. Specificity of elastase for cleavage of polypeptide chains behind the L-Ala residues was reflected in faster degradation of L-Ala-containing copolymers as well as of hydrogels composed of them.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CD - Makromolekulární chemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

Journal of Materials Science-Materials in Medicine

ISSN

0957-4530

e-ISSN

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Svazek periodika

22

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

8

Strana od-do

781-788

Kód UT WoS článku

000290044000004

EID výsledku v databázi Scopus

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