[Raman spectroscopic study of human serum albumin interacting with 3-picolylamine].

Raman spectra of human serum albumin (HSA) and HSA-3-picolylamine complex were obtained. The spectra indicate the configuration and structural transformations of HSA. The results show that the secondary structure is main alpha-helix, and the binding of 3-picolylamine doesn't change the secondary structure. However, the binding changes the configuration of disulfide bonds, transforms a single tryptophan residue from exposed tryptophan residues to hydrophobic environment, and alters the microenvironment of tyrosine.