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Synthesis of a New PHEMA/PEO Enzymatically Biodegradable Hydrogel
Author(s) -
Khelfallah Nawel S.,
Decher Gero,
Mésini Philippe J.
Publication year - 2006
Publication title -
macromolecular rapid communications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.348
H-Index - 154
eISSN - 1521-3927
pISSN - 1022-1336
DOI - 10.1002/marc.200600210
Subject(s) - macromonomer , subtilisin , tripeptide , polymer chemistry , chymotrypsin , chemistry , monomer , copolymer , materials science , trypsin , organic chemistry , enzyme , peptide , polymer , biochemistry
Summary: We report the synthesis of a new enzymatically degradable gel based on PHEMA and PEO crosslinking macromonomer. The crosslinker contains the tripeptide sequence Gly‐Gly‐Leu, which is a substrate for proteases such as subtilisin or chymotrypsin. The crosslinker was obtained by the coupling reaction of succinyl‐glycyl‐glycyl‐leucine with 2‐aminoethyl‐terminated PEO chains ( $\overline M _{\rm w}$ = 3 400) and subsequent esterification of the hydroxyl endgroup with methacryloyl chloride. It was characterized by SEC and 1 H NMR. Enzymatic cleavage of the crosslinking macromonomer was showed by SEC. The macromonomer was copolymerized with HEMA to yield hydrogel that is stable in a physiological buffer. Enzymatic assay showed that this gel is degraded in the presence of a bacterial protease (subtilisin). The degradation is complete within 50 d at 37 °C. This new gel is a good candidate for drug‐delivery systems where the release can be triggered by the presence of bacterial proteases.PHEMA crosslinked with MA‐PEG‐SucGGL‐PEO‐MA and its degradation by subtilisin.