Conformational changes in fibronectin due to adsorption to well-defined surface chemistries

Protein adsorption to surfaces is a complex phenomenon resulting in partial unfolding of the protein thereby changing its structure or conformation. We have shown that changes in the structure of fibronectin (Fn) upon adsorption to surfaces alter the integrin alpha(5)beta(1) binding affinity and modulate subsequent cellular events. [1] This study investigates adsorption-induced conformational changes of a well-characterized recombinant Fn fragment both kinetically and at equilibrium. The work presented here provides a mechanistic understanding of how conformational changes influence integrin binding and subsequent cell function.