Issue 42, 2013

Enzyme-triggered hydrogelation via self-assembly of alternating peptides

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

Supplementary files

Article information

Article type
Communication
Submitted
09 Mar 2013
Accepted
08 Apr 2013
First published
09 Apr 2013

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

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements