PLASMA-PROTEIN ADSORPTION TO ARTIFICIAL LIGAMENT FIBERS

The adsorption of plasma proteins onto biomedical polymers is an impor tant factor in the biocompatibility of biomaterials. We identified the plasma proteins adsorbed onto four polymeric fibers used for syntheti c ligament replacement: polyarylamide, polylactic acid, polyester, and polypropylene. The adsorbed proteins were eluted and analyzed by one- dimensional and two-dimensional gel electrophoresis. Fibrinogen, album in, IgG, high molecular weight kininogen (HMWK), and lipoproteins ApoA -1 and ApoE were the major proteins adsorbed onto polyarylamide. The t hree others biomaterials bound albumin, fibrinogen, ApoA-1, and ApoE;h owever, the proportions of proteins bound to each polymer differed. Th ere was an inverse relationship between ApoA-1 and fibrinogen binding for all four biomaterials; polyarylamide bound a high percentage of fi brinogen, but little ApoA-1; polylactic acid, polyester, and polypropy lene bound a high percentage of ApoA-1, but little fibrinogen. These r esults support suggestions that low fibrinogen adsorption might be due to the preferential adsorption of Apo-1. High fibrinogen binding to p olyarylamide ligaments may favor fibroblast adherence, growth, and tis sue repair. (C) 1995 John Wiley & Sons, inc.