Poly (vinyl alcohol) (PVA) hydrogel is one of the anticipated materials for artificial cartilage. In our previous studies, wear of PVA hydrogel depended on content of proteins in lubricants. The secondary structures of bovine serum albumin (BSA) and human gamma globulin (HGG) were investigated in circular dichroism spectroscopy to clarify the influence of the proteins on frictional properties. BSA and HGG were mainly composed of the α-helix and the β-sheet, respectively. BSA containing the α-helix structure showed low friction compared to HGG composed of the β-sheet structure in mixed or boundary lubrication mode. The α-helix structure forms low shear layer because the α-helix structure is easily released from surfaces and low cohesive strength. HGG forms uniform adsorption layer, but showed higher friction than BSA in the rubbing with single protein. In the repeated rubbing with changing of lubricants from HGG to BSA, however, the final friction was reduced, because an optimum layered structure of proteins was formed. Hence, layered structure of proteins appears to play an important role to protect rubbing surfaces and to reduce friction. In heat treatment tests, heat-induced BSA showed very low friction because of reduction of the α-helix structure. Heat-induced HGG did not show large differences from native HGG, but could not bring low friction with heat-induced BSA. Thus it was shown that the protein conformation has effective influences on friction.
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