| 光谱学与光谱分析 |
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| Raman Spectroscopic Study of Human Serum Albumin Interacting with 3-Picolylamine |
| GUO Jian-yu1,SUN Zhen-rong1*,WU Liang-ping1,LI Rong-xiu2,WANG Zu-geng1 |
1. Key Laboratory of Optical and Magnetic Resonance Spectroscopy, East China Normal University, Shanghai 200062, China
2. Shanghai Research Center of Biotechnology, Chinese Academy of Sciences, Shanghai 200233, China |
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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 α-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.
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Received: 2004-12-26
Accepted: 2005-06-06
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Corresponding Authors:
SUN Zhen-rong
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| Cite this article: |
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GUO Jian-yu,SUN Zhen-rong,WU Liang-ping, et al. Raman Spectroscopic Study of Human Serum Albumin Interacting with 3-Picolylamine[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(03): 460-462.
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| URL: |
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https://www.gpxygpfx.com/EN/Y2006/V26/I03/460 |
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