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Collagen-binding proteins: insights from the Collagen Toolkits.

Accepted version
Peer-reviewed

Type

Article

Change log

Authors

Farndale, Richard W  ORCID logo  https://orcid.org/0000-0001-6130-8808

Abstract

The Collagen Toolkits are libraries of 56 and 57 triple-helical synthetic peptides spanning the length of the collagen II and collagen III helices. These have been used in solid-phase binding assays to locate sites where collagen receptors and extracellular matrix components bind to collagens. Truncation and substitution allowed exact binding sites to be identified, and corresponding minimal peptides to be synthesised for use in structural and functional studies. 170 sites where over 30 proteins bind to collagen II have been mapped, providing firm conclusions about the amino acid distribution within such binding sites. Protein binding to collagen II is not random, but displays a periodicity of approximately 28 nm, with several prominent nodes where multiple proteins bind. Notably, the vicinity of the collagenase-cleavage site in Toolkit peptide II-44 is highly promiscuous, binding over 20 different proteins. This may reflect either the diverse chemistry of that locus or its diverse function, together with the interplay between regulatory binding partners. Peptides derived from Toolkit studies have been used to determine atomic level resolution of interactions between collagen and several of its binding partners and are finding practical application in tissue engineering.

Description

Keywords

binding sites, extracellular matrix, periodicity, receptor, synthetic peptide, triple helix, Amino Acid Sequence, Binding Sites, Carrier Proteins, Collagen, Humans, Peptide Library, Protein Binding

Journal Title

Essays Biochem

Conference Name

Journal ISSN

0071-1365
1744-1358

Volume Title

63

Publisher

Portland Press Ltd.

Rights

All rights reserved
Sponsorship
Wellcome Trust (094470/Z/10/Z)
Medical Research Council (G0400701)
Medical Research Council (G0500707)
British Heart Foundation (RG/15/4/31268)