Issue 30, 2012

Peptides that anneal to natural collagen in vitro and ex vivo

Abstract

Collagen comprises ¼ of the protein in humans and ¾ of the dry weight of human skin. Here, we implement recent discoveries about the structure and stability of the collagen triple helix to design new chemical modalities that anchor to natural collagen. The key components are collagen mimetic peptides (CMPs) that are incapable of self-assembly into homotrimeric triple helices, but are able to anneal spontaneously to natural collagen. We show that such CMPs containing 4-fluoroproline residues, in particular, bind tightly to mammalian collagen in vitro and to a mouse wound ex vivo. These synthetic peptides, coupled to dyes or growth factors, could herald a new era in assessing or treating wounds.

Graphical abstract: Peptides that anneal to natural collagen in vitro and ex vivo

Supplementary files

Article information

Article type
Paper
Submitted
25 1 2012
Accepted
21 3 2012
First published
23 3 2012

Org. Biomol. Chem., 2012,10, 5892-5897

Peptides that anneal to natural collagen in vitro and ex vivo

S. Chattopadhyay, C. J. Murphy, J. F. McAnulty and R. T. Raines, Org. Biomol. Chem., 2012, 10, 5892 DOI: 10.1039/C2OB25190F

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