Michel Deyme1, Adam Baszkin1, J. E. Proust1, Éric Perez1, G. Albrecht1, Marie Martine Boissonnade1
1Physico‐Chimie des Surfaces et Innovation en Pharmacotechnie, UA CNRS 1218, Université Paris‐Sud, 92290 Châtenay‐Malabry, France
Tóm tắt
AbstractAdsorption of chemically radiolabeled [14C] collagen from binary mixtures with albumin or fibrinogen was studied on the solution/air and solution/polyethylene interfaces and revealed the preferential adsorption of albumin. This phenomenon is confirmed by the data of surface tension measurements of single protein, collagen‐albumin, and collagen‐fibrinogen solutions. Desorption experiments clearly show that more irreversibly adsorbed collagen was found on polyethylene surfaces when adsorption was performed from collagen‐fibrinogen than from collagen‐albumin solutions. The combined adsorption‐desorption and the surface tension data show that competitive adsorption of collagen at the hydrophobic surfaces is strongly influenced by the surface tension properties of the proteins in solution.
