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Atomic force microscopy (AFM) was used to study the competitive adsorption betweenbovine serum albumin (BSA) and type Ⅰ collagen on hydrophilic and hydrophobic silicon wafers.BSA showed a grain shape and the type Ⅰ collagen displayed fibril-like molecules with relativelyhomogeneous height and width, characterized with clear twisting (helical formation). These AFMimages illustrated that quite a lot of type Ⅰ collagen appeared in the adsorption layer on hydrophilicsurface in a competitive adsorption state, but the adsorption of BSA was more preponderant than thatof type Ⅰ collagen on hydrophobic silicon wafer surface. The experiments showed that theinfluence of BSA on type Ⅰ collagen adsorption on hydrophilic surface was less than that onhydrophobic surface.
Atomic force microscopy (AFM) was used to study the competitive adsorption between bovine serum albumin (BSA) and type I collagen on hydrophilic and hydrophobic silicon wafers. BSA showed a grain shape and the type I collagen displayed fibril-like molecules with relatively heterogeneous height and width These AFMimages illustrated that quite a lot of type I collagen were in the adsorption layer state, but the adsorption of BSA was more preponderant than that of type I collagen on hydrophobic silicon The experiments showed that the effect of BSA on type I collagen adsorption on hydrophilic surface was less than that on hydrophrophobic surface.