Enzyme-triggered hydrogelation via self-assembly of alternating peptides

被引：58

作者：

Qin, Xu ^{[1
]}

Xie, Wenchun ^{[1
]}

Tian, Sai ^{[1
]}

Cai, Jiali ^{[1
]}

Yuan, Han ^{[1
]}

Yu, Zheng ^{[1
]}

Butterfoss, Glenn L. ^{[2
]}

Khuong, Anne C. ^{[1
]}

Gross, Richard A. ^{[1
]}

机构：

[1] NYU, Polytech Inst, Ctr Biocatalysis & Bioproc Macromol, Brooklyn, NY 11201 USA

[2] NYU, Ctr Genom & Syst Biol, New York, NY 10003 USA

来源：

CHEMICAL COMMUNICATIONS | 2013年 / 49卷 / 42期

基金：

美国国家科学基金会;

关键词：

PROTEASE-CATALYZED OLIGOMERIZATION; ACID DIETHYL ESTER; SUPRAMOLECULAR HYDROGEL; ETHYL-ESTER; SEQUENCE;

D O I：

10.1039/c3cc41794h

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

alpha-Chymotrypsin catalyzed oligomerization of the "dipeptide lego" KL-ethyl ester (OEt) in aqueous media triggers a rapid sol-gel transition due to formation of alternating (KL)(x). Resulting mixed chain oligomers, at alkaline pH, self-assemble into beta-sheets. Thereafter, intermolecular backbone hydrogen bonding between peptides causes formation of physically entangled nanofibrillar networks.

引用

页码：4839 / 4841

页数：3

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