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.

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