title: 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.
authors.affiliation: Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706, USA.
authors.forename: Sayani
authors.initials: S
authors.lastname: Chattopadhyay
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Murphy
authors.forename: Jonathan F
authors.initials: JF
authors.lastname: McAnulty
authors.forename: Ronald T
authors.initials: RT
authors.lastname: Raines
mesh_terms: D000818:Animals; D003094:Collagen / Q000737:chemistry / Q000378:metabolism*; D015195:Drug Design; D005347:Fibroblasts / Q000187:drug effects; D005782:Gels; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D057786:Peptidomimetics / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism* / Q000633:toxicity; D017433:Protein Structure, Secondary
chemical_list: D005782:Gels; D057786:Peptidomimetics; D003094:Collagen