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

Zhao Wang; Yiwen Li; Yuran Huang; Matthew P Thompson; Clare L M LeGuyader; Swagat Sahu; Nathan C Gianneschi

doi:10.1039/c5cc05653e

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

Chem Commun (Camb). 2015 Dec 14;51(96):17108-11. doi: 10.1039/c5cc05653e.

Authors

Zhao Wang¹, Yiwen Li¹, Yuran Huang², Matthew P Thompson¹, Clare L M LeGuyader¹, Swagat Sahu¹, Nathan C Gianneschi²

Affiliations

¹ Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Dr., La Jolla, CA 92093, USA. ngianneschi@ucsd.edu.
² Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Dr., La Jolla, CA 92093, USA. ngianneschi@ucsd.edu and Materials Science and Engineering, University of California, San Diego, 9500 Gilman Dr., La Jolla, CA 92093, USA.

PMID: 26452255
DOI: 10.1039/c5cc05653e

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.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

MeSH terms

Micelles
Peptide Hydrolases / metabolism*
Peptides, Cyclic / chemistry
Peptides, Cyclic / metabolism*
Polymerization
Polymers / chemistry
Polymers / metabolism*
Temperature

Substances

Micelles
Peptides, Cyclic
Polymers
Peptide Hydrolases