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Journal of Materials Chemistry B Vol -3

Journal of Materials Chemistry B Vol -2

Journal of Materials Chemistry B Vol -1

Enzyme–substrate interactions promote the self-assembly of amino acid derivatives into supramolecular hydrogels

Content Provider	Royal Society of Chemistry (RSC)
Author	Wang, Yuefei Su, Rongxin Xie, Yanyan He, Zhimin Qi, Wei Huang, Renliang
Copyright Year	2016
Abstract	Enzyme-responsive supramolecular hydrogels are a new class of smart materials and have enormous potential to be used in biology and medicine. In this study, α-chymotrypsin was proposed to promote the self-assembly of amino acid derivatives for the preparation of such supramolecular hydrogels. It is found that α-chymotrypsin significantly shortens the gelation time from 8 days (or no gelation occurred within 2 weeks) to 10 min–4 h depending on the structure of amino acid derivatives. The chemical compositions and microstructures of the hydrogels were further investigated by LC-MS, microscopy and spectroscopy techniques. The results show that the transparent hydrogels consist of long nanofibers with approximately 20 nm in diameter. These nanofibers are composed of Fmoc-amino acid and amino acid, which were formed from the hydrolysis of amino acid ester, with a molar ratio of 4.346 : 1 (Fmoc-F/F) and 0.548 : 1 (Fmoc-F/Y), respectively. Furthermore, the molecular simulation was performed to investigate the specific recognition of α-chymotrypsin to amino acid derivatives. The results indicate that the enzyme–substrate interactions are responsible for promoting the supramolecular self-assembly of these amino acid derivatives into fibrous hydrogels. In addition to being the first example of enzyme–substrate interaction-promoted supramolecular self-assembly, this novel concept opens up the possibility of making use of various enzymes and their substrates (or analogues) in the discovery of new supramolecular materials with enzyme responsiveness.
Starting Page	844
Ending Page	851
Page Count	8
File Format	HTM / HTML PDF
ISSN	2050750X
Volume Number	4
Issue Number	5
Journal	Journal of Materials Chemistry B
DOI	10.1039/c5tb02149a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Molecular biology Self-assembly Carboxylic acid Microscopy Spectroscopy Hydrolysis Ester Concentration Enzyme
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Materials Science Biomedical Engineering

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