Changes in Albumin/Platelet Interaction with an Artificial Surface—Due to Antibiotics, Pyridoxal Phosphate, and Lymphocytes

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Abstract
Protein adsorption and platelet adhesion are two important biological processes arising at the blood prosthetic interface. The effect of certain antibiotics, namely, neomycin, gentamicin, ampicillin, penicillin-G, and streptomycin to modulate the ablumin polycarbonate surface interaction was investigated using 125I albumin from a protein mixture in the presence and absence of isolated calf lymphocytes. This study also demonstrated the changes in platelet-surface adhesion with these antibiotics. The effect of pyridoxal phosphate to modulate the red blood cell-mediated platelet-surface attachment was also attempted. It appears from pyridoxal phosphate studies that pyridoxal 5''-phosphate (PLP) could modify the surface-platelet attachment. It also inhibited the fibrinogen-induced platelet adhesion. It seems, the addition of antibiotics to the polymerprotein system increased the level of surface-bound albumin variably whereas lymphocytes incubated in the medium did not affect the surface-albumin concentration with time course. These antibiotics also inhibited the surface-induced platelet adhesion to variable degrees. Our earlier studies have indicated that certain antibiotics or antiplatelet drugs can inhibit the fibrogen binding to an artificial surface. Therefore, it may be possible that the enhanced albumin-surface concentration or reduced fibrinogen-surface binding, in the presence of these antibiotics, may itself be one of the parameters for a reduced platelet-surface attachment, which may also improve the blood compatibility of the substrate. A better understanding of the mechanism of antibiotics is needed in in vivo conditions to correlate these findings.