Interaction Between Baicalein and Amyloid-β Fibrils Studied by Fluorescence Spectroscopy

doi:10.1007/s40242-013-2180-1

高等学校化学研究 ›› 2013, Vol. 29 ›› Issue (1): 20-25.doi: 10.1007/s40242-013-2180-1

Interaction Between Baicalein and Amyloid-β Fibrils Studied by Fluorescence Spectroscopy

SONG Sheng-mei^1,2, WANG Yong-xiang², XIONG Li-min², QU Ling-bo¹, XU Mao-tian^1,2

1. Department of Chemistry, Zhengzhou University, Zhengzhou 450052, P. R. China;
2. Key Laboratory Cultivation Base of Nanobiological Analytical Chemistry of Henan Province, College of Chemistry and Chemical Engineering, Shangqiu Normal University, Shangqiu 476000, P. R. China

收稿日期:2012-05-07 修回日期:2012-07-01 出版日期:2013-02-01 发布日期:2013-01-23
基金资助:
Supported by the National Natural Science Foundation of China(Nos.21175091, 21205076) and the Key Scientific and Technological Project of Henan Province, China(No.122102310478).

Interaction Between Baicalein and Amyloid-β Fibrils Studied by Fluorescence Spectroscopy

SONG Sheng-mei^1,2, WANG Yong-xiang², XIONG Li-min², QU Ling-bo¹, XU Mao-tian^1,2

1. Department of Chemistry, Zhengzhou University, Zhengzhou 450052, P. R. China;
2. Key Laboratory Cultivation Base of Nanobiological Analytical Chemistry of Henan Province, College of Chemistry and Chemical Engineering, Shangqiu Normal University, Shangqiu 476000, P. R. China

Received:2012-05-07 Revised:2012-07-01 Online:2013-02-01 Published:2013-01-23
Supported by:
Supported by the National Natural Science Foundation of China(Nos.21175091, 21205076) and the Key Scientific and Technological Project of Henan Province, China(No.122102310478).

摘要/Abstract

摘要：

The interaction between baicalein and amyloid-β(Aβ) polypeptide was investigated by fluorescence and UV-Vis absorbance spectroscopy. The absence of the characteristic peak of tyrosinate(Tyr) in the absorption spectra of Aβ-baicalein complexes provided evidence that the sole Tyr residue in Aβ is not bound to baicalein, but remains close to it. The intrinsic fluorescence of Tyr residues in Aβ_1―42 aggregates was quenched strongly by the excited-state ionization of baicalein. In this complex the hydroxyl group was not ionized, but to ionize immediately upon excitation. Absorbance, fluorescence and synchronous spectroscopies show that the formation of Schiff base between the quinone of baicalein and the lysine(Lys) side chains of Aβ_1―42 is another major reason in the depolymerization of Aβ_1―42 aggregates by baicalein. It is desirable that our research would offer some valuable reference for the application of flavonoid derivants in Alzheimer's disease(AD) treatment.

关键词: Amyloid-β peptide, Baicalein, Depolymerization, Molecular mechanism, Fluorescence spectroscopy

Abstract:

Key words: Amyloid-β peptide, Baicalein, Depolymerization, Molecular mechanism, Fluorescence spectroscopy

SONG Sheng-mei, WANG Yong-xiang, XIONG Li-min, QU Ling-bo, XU Mao-tian. Interaction Between Baicalein and Amyloid-β Fibrils Studied by Fluorescence Spectroscopy[J]. 高等学校化学研究, 2013, 29(1): 20-25.

SONG Sheng-mei, WANG Yong-xiang, XIONG Li-min, QU Ling-bo, XU Mao-tian. Interaction Between Baicalein and Amyloid-β Fibrils Studied by Fluorescence Spectroscopy[J]. Chemical Research in Chinese Universities, 2013, 29(1): 20-25.

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Interaction Between Baicalein and Amyloid-β Fibrils Studied by Fluorescence Spectroscopy

Interaction Between Baicalein and Amyloid-β Fibrils Studied by Fluorescence Spectroscopy

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