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Issue 30, 2012
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Peptides that anneal to natural collagen in vitro and ex vivo

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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

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Publication details

The article was received on 25 Jan 2012, accepted on 21 Mar 2012 and first published on 23 Mar 2012


Article type: Paper
DOI: 10.1039/C2OB25190F
Citation: Org. Biomol. Chem., 2012,10, 5892-5897
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    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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