[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.
Guo
Jian-yu
JY
Key Laboratory of Optical and Magnetic Resonance Spectroscopy, East China Normal University, Shanghai 200062, China.
Sun
Zhen-rong
ZR
Wu
Liang-ping
LP
Li
Rong-xiu
RX
Wang
Zu-geng
ZG
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
D010847:Picolines; D012709:Serum Albumin; C063598:3-(aminomethyl)pyridine