Peptides that anneal to natural collagen in vitro and ex vivo

Autor:	Jonathan F. McAnulty, Christopher J. Murphy, Sayani Chattopadhyay, Ronald T. Raines
Rok vydání:	2012
Předmět:	Models Molecular Chemistry Peptidomimetic Collagen helix Organic Chemistry Human skin Fibroblasts Biochemistry Protein Structure Secondary Article In vitro Mice Drug Design Biophysics Animals Humans Collagen Peptidomimetics Physical and Theoretical Chemistry Gels Ex vivo Triple helix
Zdroj:	Organic & Biomolecular Chemistry. 10:5892
ISSN:	1477-0539 1477-0520
DOI:	10.1039/c2ob25190f
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94204252dcad2c08d17758dbd229c0db https://doi.org/10.1039/c2ob25190f Zobrazit plný text záznamu