Issue 96, 2015
From the journal:

Chemical Communications

Enzyme-regulated topology of a cyclic peptide brush polymer for tuning assembly†

Zhao Wang,‡a   Yiwen Li,‡a   Yuran Huang,ab   Matthew P. Thompson,a   Clare L. M. LeGuyader,a   Swagat Sahua  and  Nathan C. Gianneschi*ab  

* Corresponding authors

a Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Dr., La Jolla, CA 92093, USA
E-mail: ngianneschi@ucsd.edu

b Materials Science and Engineering, University of California, San Diego, 9500 Gilman Dr., La Jolla, CA 92093, USA

Abstract

Norbornenyl cyclic elastin-like peptides were polymerized via ring opening metathesis polymerization (ROMP) to generate thermally responsive brush polymers. The thermally-responsive nature of the materials could be attenuated by the addition of a proteolytic enzyme that causes the cyclic peptide side chains to be linearized.

Graphical abstract: Enzyme-regulated topology of a cyclic peptide brush polymer for tuning assembly

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Article information

DOI
https://doi.org/10.1039/C5CC05653E
Article type
Communication
Submitted
08 Jul 2015
Accepted
23 Sep 2015
First published
09 Oct 2015

Chem. Commun., 2015,51, 17108-17111

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Enzyme-regulated topology of a cyclic peptide brush polymer for tuning assembly

Z. Wang, Y. Li, Y. Huang, M. P. Thompson, C. L. M. LeGuyader, S. Sahu and N. C. Gianneschi, Chem. Commun., 2015, 51, 17108 DOI: 10.1039/C5CC05653E

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