Enzymatic degradation of the hydrogels based on synthetic poly(α-amino acid)s
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- aminokyseliny chemie MeSH
- biodegradace MeSH
- biokompatibilní materiály chemie MeSH
- časové faktory MeSH
- chemické modely MeSH
- chrupavka patologie MeSH
- gely MeSH
- hydrogely chemie MeSH
- magnetická rezonanční spektroskopie MeSH
- methakryláty chemie MeSH
- pankreatická elastasa chemie MeSH
- peptidy chemie MeSH
- polymery chemie MeSH
- reagencia zkříženě vázaná chemie MeSH
- regenerace nervu MeSH
- tkáňové inženýrství přístrojové vybavení MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aminokyseliny MeSH
- biokompatibilní materiály MeSH
- gely MeSH
- hydrogely MeSH
- hydroxyethyl methacrylate MeSH Prohlížeč
- methakryláty MeSH
- pankreatická elastasa MeSH
- peptidy MeSH
- polymery MeSH
- reagencia zkříženě vázaná MeSH
Biodegradable hydrogels are studied as potential scaffolds for soft tissue regeneration. In this work biodegradable hydrogels were prepared from synthetic poly(α-amino acid)s, poly(AA)s. The covalently crosslinked gels were formed by radical copolymerization of methacryloylated poly(AA)s, e.g. poly[N (5)-(2-hydroxy-ethyl)-L-glutamine-ran-L-alanine-ran-N (6)-methacryloyl-L-lysine], as a multifunctional macro-monomer with a low-molecular-weight methacrylic monofunctional monomer, e.g. 2-hydroxyethyl methacrylate (HEMA). Methacryloylated copolypeptides were synthesized by polymerization of N-carboxyanhydrides of respective amino acids and subsequent side-chain modification. 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-alanine residues was reflected in faster degradation of L-alanine-containing copolymers as well as of hydrogels composed of them.
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