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Integrin α v β 3  expression is altered in various diseases and has been proposed as a drug target. Here we use a rational design approach to develop a therapeutic protein, which we call ProAgio, that binds to integrin α v β 3  outside the classical ligand-binding site. We show ProAgio induces apoptosis of integrin α v β 3 -expressing cells by recruiting and activating caspase 8 to the cytoplasmic domain of integrin α v β 3 . ProAgio also has anti-angiogenic activity and strongly inhibits growth of tumour xenografts, but does not affect the established vasculature. Toxicity analyses demonstrate that ProAgio is not toxic to mice. Our study reports a new integrin-targeting agent with a unique mechanism of action, and provides a template for the development of integrin-targeting therapeutics.

Rational design of a protein that binds integrin αvβ3 outside the ligand binding site