Abstract
Serum albumin is the most abundant protein in mammalian plasma and is often used as a model to understand the adhesion behavior of proteins on surfaces. Attenuated total reflection-Fourier transform infrared spectroscopy (ATR-FTIR) is used to non-destructively and dynamically detect the chemical change information between the protein and the surface during the adhesion process, which is especially suitable for in-situ measurement of samples in water. Therefore, the adhesion of bovine serum albumin (BSA) on the surface in H2O and D2O is investigated by ATR-FTIR technology, which effectively avoids the interference of the characteristic peak of deformation vibration of liquid H2O (1645 cm−1) on the amide I band of BSA. Sodium alginate, a polysaccharide widely present in the ocean, is introduced into the BSA solution to explore the changes in the adhesion process of proteins on the surface of ZnSe, and polarized ATR-FTIR spectra are also collected to study the adhesion orientation of BSA. Sodium alginate presents a negative effect on the adhesion of BSA on the surface and there is no specific orientation of BSA on the surface.
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