Spectroscopic Study of Binding Reaction between Celastrol and Bovine Serum Albumin

doi:10.7506/spkx1002-6630-200917030

FOOD SCIENCE ›› 2009, Vol. 30 ›› Issue (17 ): 130-133.doi: 10.7506/spkx1002-6630-200917030

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Spectroscopic Study of Binding Reaction between Celastrol and Bovine Serum Albumin

ZHANG Ting1，XU Hui2，LI Gui-hua2，LIU Cheng-yin3，ZOU Ning1，ZHANG Xin2，LIU Quan-wen2,*

1. College of Life Science, Ludong University, Yantai 264025, China；2. College of Chemistry and Materials Science, Ludong
University, Yantai 264025, China；3. Department of Biology, The First Middle School of Qixia City, Qixia 265300, China

Received:2009-06-10 Online:2009-09-01 Published:2014-04-14
Contact: LIU Quan-wen E-mail:qwliu2001@yahoo.com.cn

Abstract

Abstract:

Fluorescent and UV-vis spectroscopic methods were adopted to study the binding reaction of celastrol (CSL) with bovine serum albumin (BSA). The quenching of BSA by CSL was found to a static process. The primary binding pattern between celastrol and BSA was interpreted as hydrophobic interaction with the binding ratio of 1:1 under physiological conditions. It was found that celastrol was located near the Tyr residue region of site I in BSA by competitive binding experiments using warfarin and ibuprofen as site markers. The distance between the donor (BSA) and receptor (celastrol), r, was calculated to be 2.31 nm according to Frster's non-radiative energy transfer theory. In addition, the effect of celastrol on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy.

Key words: celastrol, bovine serum albumin, interaction, competitive binding experiment

CLC Number:

ZHANG Ting1，XU Hui2，LI Gui-hua2，LIU Cheng-yin3，ZOU Ning1，ZHANG Xin2，LIU Quan-wen2,*. Spectroscopic Study of Binding Reaction between Celastrol and Bovine Serum Albumin[J]. FOOD SCIENCE, 2009, 30(17 ): 130-133 https://doi.org/10.7506/spkx1002-6630-200917030

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Spectroscopic Study of Binding Reaction between Celastrol and Bovine Serum Albumin

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