Protein-protein interactions affecting proteins at surfaces

Protein adsorption to methylated silicon gradient and hydrophilic silicon surfaces as single, binary, and tertiary purified components as well as in association with normal plasma were studied. Antibody and albumin incubations of protein and plasma treated surfaces were noted to affect ellipsometric thickness and antibody binding patterns. BSA blocking procedures on surfaces treated with pure fibrinogen were able to mimic, to a degree, the same ellipsometric patterns as plasma treated gradients when probed by specific antibodies. Indications are that serum albumin influences and may even participate in the removal of IgG and fibrinogen from certain surfaces, even as a subsequent, non-competitive step. HMWK adsorbs differently to surfaces dependent on whether it is a serum component or a single protein. Specific antibody incubations of protein and plasma treated surfaces have been observed to cause a reduction in the ellipsometrically observable surface bound protein layer. These relationships may be due to components other than those indicated by the Vroman sequence.