Abstract

Professor Richard Farndale is head of a Molecular Cell Biology group in the Department of Biochemistry. His work centers on understanding how collagen, the most abundant protein in the vertebrate organism, interacts with other proteins. Up to the last three or four years, work has focused on the platelet collagen receptors, integrin alpha2beta1 and Glycoprotein VI, with a view to elucidating the processes which mediate thrombus formation in coronary artery disease. Triple-helical peptides have been synthesised whose sequence is specific for these receptors. Recently, triple-helical peptide libraries have been produced which embrace the whole of the sequence of collagens II and III . These allow the binding of any of collagen’s many partners to be mapped systematically, allowing identification of the sites that bind von Willebrand factor, completing understanding of the platelet-collagen interaction, and the Discoidin Domain Receptor tyrosine kinases, DDR1 and DDR2 , as well as other non-receptor species, including fibronectin and SPARC . This understanding allows specific ligands for each of these species to be made, although several of these species have been found to bind hot-spots within the tropocollagen molecule. Peptides are now being designed with which to decorate matrix scaffolds for tissue-engineering use, and so enhance their interaction with the extracellular matrix and cell-surface receptors.