Conformational states of fibronectin. Effects of pH, ionic strength, and collagen binding.

Human plasma fibronectin was enzymatically labeled with dansylcadaverine using plasma Factor XIIa. Fluorescence polarization studies of dansylcadaverine-labeled fibronectin indicate that fibronectin has a significant degree of chain flexibility in physiologic solution and that there is an increase in chain flexibility at high pH or ionic strength. Binding of a collagen peptide to dansylcadaverine-fibronectin results in a decrease in fluorescence polarization, suggesting that such binding causes a conformational change which also results in increased chain flexibility.l Quasielastic light scattering and intrinsic viscosity measurements of fibronectin were performed under physiologic conditions and at high pH and ionic strength. Shape calculations based on these data indicate that fibronectin is in an elongated configuration under physiologic conditions and further unfolds at high pH or ionic strength into a very flexible, strand-like configuration. Light scattering studies of fibronectin after binding of a collagen fragment indicate that such binding results in a decrease in the diffusion coefficient, suggesting that collagen binding also results in a partial unfolding of fibronectin. These results suggest that published electron micrographs of fibronectin showing a long, strand-like molecule do not reflect the conformation of plasma fibronectin under physiologic conditions; fibronectin, however, may assume an unfolded conformation upon binding to collagen in the tissue matrix.