Abstract
The interfacial exchange processes between human serum albumin (HSA) and fibrinogen on different surfaces was investigated with in situ ellipsometry and total internal reflectance fluorescence (TIRF) spectroscopy. With ellipsometry, it was found that the total absorbed amount on silica on the addition of fibrinogen after the preadsorption of HSA was quite similar to that obtained without HSA preadsorption. From TIRF, it was concluded that the preadsorbed HSA is displaced, although not completely, on the addition of fibrinogen. On the other hand, preadsorbed HSA effectively blocked further adsorption of fibrinogen and IgG on hydrophobic surfaces such as methylated silica. Furthermore, the competitive adsorption of HSA and fibrinogen on two phospholipid surfaces, i.e. phosphatidylcholine (PC) and phosphatidic acid (PA), was investigated. It was found that on PA, fibrinogen adsorbs extensively even after the preadsorption of HSA. This, however, is achieved with essentially no displacement of the preadsorbed HSA. For PC, finally, the fibrinogen adsorption is much lower than that of HSA, and fibrinogen is able neither to coadsorb with HSA nor to displace the preadsorbed protein.
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