RESEARCH PAPER
Influence of Hydrogen Bond and Sodium Alginate on Bovine Serum Albumin Adhesion on ZnSe Surface

https://doi.org/10.1016/S1872-2040(21)60101-9Get rights and content

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.

Graphical abstract

The adhesion changes of bovine serum albumin (BSA) on the ZnSe crystal surface under the influence of D2O and sodium alginate are investigated by ATR-FTIR technology, especially to study the secondary structure content changes.

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    This work was supported by the National Natural Science Foundation of China (No. 21675165).

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