Principles governing biomolecule interactions at foreign interfaces

Abstract

Abstract The adsorption, conformational changes, and desorption of biological molecules at foreign interfaces are effected by both kinetic and thermodynamic factors. The thermodynamic factors which drive the biomolecule/foreign interface system towards equilibrium include the enthalpy and entropy changes occurring during each step in the adsorption process. The principles governing interaction of proteins with nonwettable (nonpolar) and wettable (polar) foreign interfaces are discussed in terms of these thermodynamic parameters. Some examples to illustrate these arguments are presented are presented for plasma‐protein interactions on Silastic and radiation‐grafted hydrogel/Silastic interfaces.