ScholarLens Back to search
2009•Journal of Instrumental AnalysisRequires access

Effect of Hydroxyl Substituent on the Interactions between Three Flavonoids and Bovine Serum Albumin

Xinyu Jiang

Open publisher page 0 citations

Abstract

Fluorescence spectroscopy was used to investigate the interactions of bovine serum albumin(BSA) with flavonoids apigenin(Api),genistein(Gen) and galangin(Gal).The fluorescence quenching mechanism of BSA by each compound was studied.The binding constant and binding site number were also measured.The result indicated that BSA was reacted with each compound by hydrophobic force and static quenching mode.The influence of Api,Gen and Gal on the conformation of BSA was investigated using synchronous fluorescence and UV absorption spectroscopy.The interaction strength order of the compounds and BSA was as follows:ApiGalGen,which indicated that the number and site of substituted hydroxyl in each molecule played an important role in the interaction of these compounds with BSA.

About this research paper

What this paper is about

Fluorescence spectroscopy was used to investigate the interactions of bovine serum albumin(BSA) with flavonoids apigenin(Api),genistein(Gen) and galangin(Gal).The fluorescence quenching mechanism of BSA by each compound was studied.The binding constant and binding site number were also measured.The result indicated that BSA was reacted with each compound by hydrophobic force and static quenching mode.The influence of Api,Gen and Gal on the conformation of BSA was investigated using synchronous fluorescence and UV absorption spectroscopy.The interaction strength order of the compounds and BSA was as follows:ApiGalGen,which indicated that the number and site of substituted hydroxyl in each molecule played an important role in the interaction of these compounds with BSA.

Why it matters

A significance statement is not available in the OpenAlex record.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Fluorescence spectroscopy was used to investigate the interactions of bovine serum albumin(BSA) with flavonoids apigenin(Api),genistein(Gen) and galangin(Gal).The fluorescence quenching mechanism of BSA by each compound was studied.The binding constant and binding site number were also measured.The result indicated that BSA was reacted with each compound by hydrophobic force and static quenching mode.The influence of Api,Gen and Gal on the conformation of BSA was investigated using synchronous fluorescence and UV absorption spectroscopy.The interaction strength order of the compounds and BSA was as follows:ApiGalGen,which indicated that the number and site of substituted hydroxyl in each molecule played an important role in the interaction of these compounds with BSA.

Key concepts: Chemistry, Bovine serum albumin, Substituent, Apigenin, Galangin, Fluorescence spectroscopy, Fluorescence, Binding constant

Related papers

Related paper 1Related paper 2Related paper 3
Back to paper searchBrowse research topicsOriginal source
Effect of Hydroxyl Substituent on the Interactions between Three Flavonoids and Bovine Serum Albumin — Research Paper | ScholarLens