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Journal of Biochemistry Advance Access published online on November 2, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp175
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy

Takuhiro Otosu, Etsuko Nishimoto and Shoji Yamashita*

Institute of Biophysics, Faculty of Agriculture, Graduate School of Kyushu University, Hakozaki, Fukuoka 812-8581, Japan

*To whom correspondence should be addressed: Shoji Yamashita Tel/Fax: +81-92-642-4425. E-mail: yamashita{at}brs.kyushu-u.ac.jp

Received July 2, 2009; Accepted September 25, 2009


  Abstract

Human serum albumin (HSA) plays important roles for transport of fatty acids and for binding a variety of drugs and organic compounds in the circulatory system. This protein experiences several conformational transitions by the change of pH, and the resulting conformations were essential for completing the physiological roles in vivo. Steady-state and time-resolved fluorescence spectroscopy was applied to single tryptophan residue solely arranged in HSA to study subtle conformational change around single tryptophan residue in HSA at various pH. The results showed the characteristic feature of local conformation around tryptophan residue in domain II responding to the change in entire structure. The study of time-resolved area-normalized fluorescence emission spectra (TRANES) also showed the peculiar dielectric property of water molecule trapped nearby tryptophan residue depending on pH. These results suggested that microenvironment around tryptophan residue was tightly packed at acidic and basic pH although entire conformation was loosened.

Key Words: Human serum albumin (HSA), ANS fluorescence, time-resolved area-normalized fluorescence emission spectra (TRANES), time-resolved fluorescence decay, time-resolved fluorescence anisotropy


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