Abstract:
The effect of a surgical laser on the physicochemical properties of molecules of two model proteins was studied: human immunoglobulin IgG and bovine serum albumin. After exposure to laser radiation, the optical density of protein solutions changes, the fluorescence intensity decreases, and the refractive index of the solutions does not change significantly. No massive damage or ruptures of the protein polypeptide chain were observed; on the contrary, intense aggregation of protein molecules was recorded. Thus, when exposed to a laser scalpel, partial denaturation and aggregation processes prevail in IgG and bovine serum albumin solutions, and aromatic amino acid residues are damaged to a lesser extent.
