2019 Volume 139 Issue 6 Pages 128-131
Conformation and activity control of proteins adsorbed on certain material surfaces enables the development of numerous high-performance applications. Previously, we examined the relationship between the diameter (surface shape) of polyurethane (PU) nanofibers and the conformation/activity of adsorbed protein. Proteins adsorbed on thick nanofibers (diameter: 950 nm) showed decreased activity due to large conformational changes, whereas those adsorbed on thin nanofibers (diameter: 480 nm) retained a close-to-natural shape and thus showed relatively high activity, confirming that the shape of PU nanofiber surface affects the conformation and activity of proteins adsorbed thereon. In this study, in order to prove this hypothesis, the adsorption strength of the adsorbed protein onto the polyurethane nanofiber was evaluated. As a result, it was confirmed that proteins adsorbed on thick nanofibers have higher adsorption strength than thin nanofibers. These results suggested that the thickness of the nanofibers determines the adsorption area between molecule and nanofiber surface, and affects the structure and activity of the adsorbed protein.
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