Issue 42, 2013
From the journal:

Chemical Communications

Enzyme-triggered hydrogelation via self-assembly of alternating peptides†

Xu Qin,a   Wenchun Xie,a   Sai Tian,a   Jiali Cai,a   Han Yuan,a   Zheng Yu,a   Glenn L. Butterfoss,b   Anne C. Khuonga  and  Richard A. Gross*a  

* Corresponding authors

a Center for Biocatalysis and Bioprocessing of Macromolecules, The Polytechnic Institute of New York University, Six Metrotech Center, Brooklyn, New York 11201, USA
E-mail: rgross@poly.edu

b Center for Genomics and Systems Biology, New York University, New York 10003, USA

Abstract

α-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 β-sheets. Thereafter, intermolecular backbone hydrogen bonding between peptides causes formation of physically entangled nanofibrillar networks.

Graphical abstract: Enzyme-triggered hydrogelation via self-assembly of alternating peptides

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Article information

DOI
https://doi.org/10.1039/C3CC41794H
Article type
Communication
Submitted
09 Mar 2013
Accepted
08 Apr 2013
First published
09 Apr 2013

Chem. Commun., 2013,49, 4839-4841

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Enzyme-triggered hydrogelation via self-assembly of alternating peptides

X. Qin, W. Xie, S. Tian, J. Cai, H. Yuan, Z. Yu, G. L. Butterfoss, A. C. Khuong and R. A. Gross, Chem. Commun., 2013, 49, 4839 DOI: 10.1039/C3CC41794H

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