A Comprehensive Evaluation of the Activity and Selectivity Profile of Ligands for RGD-binding Integrins

TLDR

Integrins are heterodimeric cell surface receptors that regulate cell morphology, proliferation, survival and differentiation, and mutations or deregulated expression are linked to many diseases, yet the IC₅₀ values of developed ligands vary widely across different assay systems. The study aims to systematically compare these IC₅₀ values to aid in selecting the most suitable ligands for specific applications. To achieve this, the authors measured the binding affinity of a broad panel of ligands to RGD‑binding integrins (αvβ3, αvβ5, αvβ6, αvβ8, α5β1, αIIbβ3) using a homogeneous ELISA‑like solid‑phase binding assay.

Abstract

Abstract Integrins, a diverse class of heterodimeric cell surface receptors, are key regulators of cell structure and behaviour, affecting cell morphology, proliferation, survival and differentiation. Consequently, mutations in specific integrins, or their deregulated expression, are associated with a variety of diseases. In the last decades, many integrin-specific ligands have been developed and used for modulation of integrin function in medical as well as biophysical studies. The IC 50 -values reported for these ligands strongly vary and are measured using different cell-based and cell-free systems. A systematic comparison of these values is of high importance for selecting the optimal ligands for given applications. In this study, we evaluate a wide range of ligands for their binding affinity towards the RGD-binding integrins αvβ3, αvβ5, αvβ6, αvβ8, α5β1, αIIbβ3, using homogenous ELISA-like solid phase binding assay.