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
收藏
页码：4839 / 4841
页数：3
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