Influence of laser radiation of a surgical laser on the structure of bovine serum albumin molecules in vitro

Abstract

The influence of laser radiation of a surgical laser on the physicochemical properties of bovine serum albumin molecules was studied. After exposure to laser radiation, the optical density of protein solutions increases, the fluorescence intensity decreases, a significant decrease of the intensity of the a-helix band on the Raman spectrum is observed and the refractive index of protein solution did not significantly change. However, the viscosity increased, and the pseudoplasticity of aqueous solutions of albumin decreased. There was no massive damage to the protein polypeptide chain, on the contrary, intensive aggregation was observed. Thus, in a bovine serum albumin solution subjected to contact action of laser radiation, the processes of partial denaturation and aggregation prevail, aromatic amino acid residues of the protein are damaged to a lesser extent, and fragmentation of albumin molecules is not observed.