title: [Raman spectroscopic study of human serum albumin interacting with 3-picolylamine].
abstract: 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.
authors.affiliation: Key Laboratory of Optical and Magnetic Resonance Spectroscopy, East China Normal University, Shanghai 200062, China.
authors.forename: Jian-yu
authors.initials: JY
authors.lastname: Guo
authors.forename: Zhen-rong
authors.initials: ZR
authors.lastname: Sun
authors.forename: Liang-ping
authors.initials: LP
authors.lastname: Wu
authors.forename: Rong-xiu
authors.initials: RX
authors.lastname: Li
authors.forename: Zu-geng
authors.initials: ZG
authors.lastname: Wang
mesh_terms: D001665:Binding Sites; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D010847:Picolines / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012709:Serum Albumin / Q000737:chemistry*; D013059:Spectrum Analysis, Raman
chemical_list: D010847:Picolines; D012709:Serum Albumin; C063598:3-(aminomethyl)pyridine