Plasma protein adsorption: the big twelve

Abstract

We have discussed the general principles of protein adsorption at solid-liquid interfaces from single component and multicomponent solutions, based on qualitative kinetic models that include mass transport considerations, initial interaction energies, surface-dependent conformational changes, and possible desorption processes. We have surveyed plasma protein components greater than one milligram per milliliter in concentration, which we call "The Big Twelve." We considered their size, concentration, diffusion coefficient, structure and function, and methods of estimating their "surface denaturability" by using bulk solution measures of denaturation and conformational change. We have suggested that the role of the carbohydrate moieties in plasma proteins may have some bearing on their adsorption properties. We further suggest that lipoproteins, because of their lipid phase transition and conformational lability at body temperature, may tend to dominate the adsorption process, particularly on mobile elastomeric polymer surfaces. We suggest that detailed consideration of the structure and characteristics of each of the proteins involved is necessary in order to begin to understand plasma adsorption processes. Detailed characterization and understanding of the solid surface in the aqueous and protein environments are also required.