期刊
JOURNAL OF BIOMATERIALS SCIENCE-POLYMER EDITION
卷 13, 期 6, 页码 691-711出版社
TAYLOR & FRANCIS LTD
DOI: 10.1163/156856202320269166
关键词
polyurethaneurea; biodegradation; chymotrypsin; L-phenylalanine; mass spectrometry
The degradation of novel biodegradable segmented polyurethanes was investigated with a view to determining the cleavage points within the polymer backbones targeted by the enzyme chymotrypsin. While the materials were developed with specific enzyme cleavage sites designed into the polymer chains, the nature of their degradation had not yet been determined. In this work, two segmented polyurethaneureas containing L-phenylalanine residues in the chain extender and two control polymers were subjected to degradation in the presence of chymotrypsin. Samples were collected for analysis over a time period from I day to 8 weeks. The degradation products from these materials were isolated using solid phase extraction and reversed phase high pressure liquid chromatography, and identified using mass and tandem mass spectrometry. Three hard segment related degradation products were identified and provide important insight into the polyurethane backbone cleavage sites. Cleavage of urea, ester and urethane bonds were observed. The results confirmed that chymotrypsin was able to cleave ester bonds adjacent to phenylalanine residues contained within the novel chain extender.
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