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Citation: MA Ping, CHI Yan-Hua, ZHUANG Jia, DENG Jian-Jun, ZHOU Lei. Spectroscopic Study on Interactions Between Human Serum Albumin and Acidic Chromic Blue K[J]. Chinese Journal of Applied Chemistry, ;2008, 25(9): 1032-1036. shu

Spectroscopic Study on Interactions Between Human Serum Albumin and Acidic Chromic Blue K

MA Ping ^a ,
CHI Yan-Hua ^a,, ,
ZHUANG Jia ^b ,
DENG Jian-Jun ^c ,
ZHOU Lei ^a

1.
a Department of Chemistry, Southwest University of Science and Technology, Mianyang, 621010;
2.
b Department of Materials Science and Engineering, Southwest Petroleum University, Chengdu;
3.
c Clinical Laboratory, Mianyang 404 Hospital, Mianyang

Corresponding author: CHI Yan-Hua,
Received Date: 1 September 2007
Available Online: 7 November 2007
Fund Project: 国家自然科学基金(2027104210776027) (2027104210776027)国家电分析化学重点实验室基金(2005007) (2005007)四川省科学技术重点攻关(03GG009-024)资助项目 (03GG009-024)

The interactions between human serum albumin(HSA) and acidic chromic blue K(ACBK) was investigated by fluorescence spectroscopy and Fourier transform infrared spectroscopy(FT-IR) under simulative physiological conditions.The quenching constants of HSA by ACBK suggested ACBK could quench the intrinsic fluorescence of HSA by static quenching.According to fluorescence resonance energy transfer(FRET),the distance and energy transfer efficiency(E) between the donor(HSA) and the acceptor(ACBK) were calculated to be 2.29 nm and 0.078,respectively.The relationship of fluorescence quenching and the changes of HSA secondary structure induced by ACBK binding was investigated by combining the results of fluorescence and FT-IR.The fluorescence results and FT-IR study suggested that hydrophobic interactions were the predominant intermolecular force and caused the secondary structure of HSA to change from α-helix and β-sheets to β-turns and random coils respectively.Upon HSA-ACBK complexing,the α-helix structure reduced by more than 9%,and the β-sheet reduced by 2%,while the β-turn increased by 6%,and the random coil increased by 5%.
- human serum albumin,
- acidic chromc blue K,
- fluorescence spectroscopy,
- fourier transform infrared spectroscopy,
- secondary structure
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