Integrins play important roles in cell adhesion and signalling, and crucially are over-expressed in certain cancer cells. The tripeptide Arg-Gly-Asp (RGD) is known to bind to integrins, and understanding exactly how they bind is obviously of fundamental importance for the development of structures with higher integrin affinities for possible therapeutic applications.
Here, Daniel Welsh and David K. Smith (University of York) investigate different ways in which the peptide ligands can be organised for multivalent binding to integrins. Although integrins only posses a single binding site they often grouped together in cell membranes, so mutlivalent binding to multiple integrins is possible. They investigate both dendritic (covalent) and self-assembly (non-covalent) strategies, finding both can be used in similar ways to enhance the binding of RGD peptides to integrins, but that the self-assembly approach appears to give rise to slightly higher affinity integrin binding.
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Comparing dendritic and self-assembly strategies to multivalency—RGD peptide–integrin interactions
Daniel J. Welsh and David K. Smith
Org. Biomol. Chem., 2011, Advance Article
DOI: 10.1039/C1OB05241A
