Structural analysis of peptide binding to integrins for cancer detection and treatment.

Abstract

Integrins are cell receptors involved in several metabolic pathways often associated with cell proliferation. Some of these integrins are downregulated during human physical development, but when these integrins are overexpressed in adult humans, they can be associated with several diseases, such as cancer. Molecules that specifically bind to these integrins are useful for cancer detection, diagnosis, and treatment. This review focuses on the structures of integrin-peptidic ligand complexes to dissect how the binding occurs and the molecular basis of the specificity and affinity of these peptidic ligands. Understanding these interactions at the molecular level is fundamental to be able to design new peptides that are more specific and more sensitive to a particular integrin. The integrin complexes covered in this review are α5β1, αIIbβ3, αvβ3, αvβ6, and αvβ8, because the molecular structures of the complex have been experimentally determined and their presence on tumor cancer cells are associated with a poor prognosis, making them targets for cancer detection and treatment.