2011•Strait Pharmaceutical JournalRequires access

Study on the interaction between fermononetin and bovine serum albumin by fluorescence spectroscopy

Hao Wang

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Abstract

To study the interaction of bovine serum albumin(BSA)with fermononetin(hq-2)by fluorescence quenching spectra and synchronous fluorescence spectra.The results indicated that the quenching type between BSA and fermononetin was static quenching.The binding constants Ka were 5.27×104L·mol-1 and the binding sites(n)were 1.The interaction between BSA with fermononetin was driven mainly by Electrostatic interaction.And the synchronous spectrum was used to investigate the conformational changes of BSA.The competitive probes,such as warfarin and ibuprofen(Site Ⅰ and Site Ⅱ probes,respectively),revealed that the binding location of fermononetin to BSA was in the site Ⅱ of the hydrophobic pocket.

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What this paper is about

To study the interaction of bovine serum albumin(BSA)with fermononetin(hq-2)by fluorescence quenching spectra and synchronous fluorescence spectra.The results indicated that the quenching type between BSA and fermononetin was static quenching.The binding constants Ka were 5.27×104L·mol-1 and the binding sites(n)were 1.The interaction between BSA with fermononetin was driven mainly by Electrostatic interaction.And the synchronous spectrum was used to investigate the conformational changes of BSA.The competitive probes,such as warfarin and ibuprofen(Site Ⅰ and Site Ⅱ probes,respectively),revealed that the binding location of fermononetin to BSA was in the site Ⅱ of the hydrophobic pocket.

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Available abstract

To study the interaction of bovine serum albumin(BSA)with fermononetin(hq-2)by fluorescence quenching spectra and synchronous fluorescence spectra.The results indicated that the quenching type between BSA and fermononetin was static quenching.The binding constants Ka were 5.27×104L·mol-1 and the binding sites(n)were 1.The interaction between BSA with fermononetin was driven mainly by Electrostatic interaction.And the synchronous spectrum was used to investigate the conformational changes of BSA.The competitive probes,such as warfarin and ibuprofen(Site Ⅰ and Site Ⅱ probes,respectively),revealed that the binding location of fermononetin to BSA was in the site Ⅱ of the hydrophobic pocket.

Key concepts: Bovine serum albumin, Quenching (fluorescence), Chemistry, Fluorescence, Binding site, Fluorescence spectroscopy, Hydrophobic effect, Binding constant

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