Evaluation of anthocyanins in Aronia melanocarpa/BSA binding by spectroscopic studies

Abstract The interaction between Anthocyanins in Aronia melanocarpa (AMA) and bovine serum albumin (BSA) were studied in this paper by multispectral technology, such as fluorescence quenching titration, circular dichroism (CD) spectroscopy and Fourier transform infrared spectroscopy (FTIR). The resu...

Full description

Bibliographic Details
Main Authors: Jie Wei, Dexin Xu, Xiao Zhang, Jing Yang, Qiuyu Wang
Format: Article
Language:English
Published: SpringerOpen 2018-05-01
Series:AMB Express
Subjects:
BSA
Online Access:http://link.springer.com/article/10.1186/s13568-018-0604-5
id doaj-0358fd216b674f4fb4a3be59ce426ec2
record_format Article
spelling doaj-0358fd216b674f4fb4a3be59ce426ec22020-11-24T21:51:47ZengSpringerOpenAMB Express2191-08552018-05-01811910.1186/s13568-018-0604-5Evaluation of anthocyanins in Aronia melanocarpa/BSA binding by spectroscopic studiesJie Wei0Dexin Xu1Xiao Zhang2Jing Yang3Qiuyu Wang4School of Life Science of Liaoning UniversitySchool of Life Science of Liaoning UniversitySchool of Life Science of Liaoning UniversitySchool of Life Science of Liaoning UniversitySchool of Life Science of Liaoning UniversityAbstract The interaction between Anthocyanins in Aronia melanocarpa (AMA) and bovine serum albumin (BSA) were studied in this paper by multispectral technology, such as fluorescence quenching titration, circular dichroism (CD) spectroscopy and Fourier transform infrared spectroscopy (FTIR). The results of the fluorescence titration revealed that AMA could strongly quench the intrinsic fluorescence of BSA by static quenching. The apparent binding constants KSV and number of binding sites n of AMA with BSA were obtained by fluorescence quenching method. The thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS), were calculated to be 18.45 kJ mol−1 > 0 and 149.72 J mol−1 K−1 > 0, respectively, which indicated that the interaction of AMA with BSA was driven mainly by hydrophobic forces. The binding process was a spontaneous process of Gibbs free energy change. Based on Förster’s non-radiative energy transfer theory, the distance r between the donor (BSA) and the receptor (AMA) was calculated to be 3.88 nm. Their conformations were analyzed using infrared spectroscopy and CD. The results of multispectral technology showed that the binding of AMA to BSA induced the conformational change of BSA.http://link.springer.com/article/10.1186/s13568-018-0604-5Anthocyanins in Aronia melanocarpaBSABinding modeCircular dichroismMolecular docking
collection DOAJ
language English
format Article
sources DOAJ
author Jie Wei
Dexin Xu
Xiao Zhang
Jing Yang
Qiuyu Wang
spellingShingle Jie Wei
Dexin Xu
Xiao Zhang
Jing Yang
Qiuyu Wang
Evaluation of anthocyanins in Aronia melanocarpa/BSA binding by spectroscopic studies
AMB Express
Anthocyanins in Aronia melanocarpa
BSA
Binding mode
Circular dichroism
Molecular docking
author_facet Jie Wei
Dexin Xu
Xiao Zhang
Jing Yang
Qiuyu Wang
author_sort Jie Wei
title Evaluation of anthocyanins in Aronia melanocarpa/BSA binding by spectroscopic studies
title_short Evaluation of anthocyanins in Aronia melanocarpa/BSA binding by spectroscopic studies
title_full Evaluation of anthocyanins in Aronia melanocarpa/BSA binding by spectroscopic studies
title_fullStr Evaluation of anthocyanins in Aronia melanocarpa/BSA binding by spectroscopic studies
title_full_unstemmed Evaluation of anthocyanins in Aronia melanocarpa/BSA binding by spectroscopic studies
title_sort evaluation of anthocyanins in aronia melanocarpa/bsa binding by spectroscopic studies
publisher SpringerOpen
series AMB Express
issn 2191-0855
publishDate 2018-05-01
description Abstract The interaction between Anthocyanins in Aronia melanocarpa (AMA) and bovine serum albumin (BSA) were studied in this paper by multispectral technology, such as fluorescence quenching titration, circular dichroism (CD) spectroscopy and Fourier transform infrared spectroscopy (FTIR). The results of the fluorescence titration revealed that AMA could strongly quench the intrinsic fluorescence of BSA by static quenching. The apparent binding constants KSV and number of binding sites n of AMA with BSA were obtained by fluorescence quenching method. The thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS), were calculated to be 18.45 kJ mol−1 > 0 and 149.72 J mol−1 K−1 > 0, respectively, which indicated that the interaction of AMA with BSA was driven mainly by hydrophobic forces. The binding process was a spontaneous process of Gibbs free energy change. Based on Förster’s non-radiative energy transfer theory, the distance r between the donor (BSA) and the receptor (AMA) was calculated to be 3.88 nm. Their conformations were analyzed using infrared spectroscopy and CD. The results of multispectral technology showed that the binding of AMA to BSA induced the conformational change of BSA.
topic Anthocyanins in Aronia melanocarpa
BSA
Binding mode
Circular dichroism
Molecular docking
url http://link.springer.com/article/10.1186/s13568-018-0604-5
work_keys_str_mv AT jiewei evaluationofanthocyaninsinaroniamelanocarpabsabindingbyspectroscopicstudies
AT dexinxu evaluationofanthocyaninsinaroniamelanocarpabsabindingbyspectroscopicstudies
AT xiaozhang evaluationofanthocyaninsinaroniamelanocarpabsabindingbyspectroscopicstudies
AT jingyang evaluationofanthocyaninsinaroniamelanocarpabsabindingbyspectroscopicstudies
AT qiuyuwang evaluationofanthocyaninsinaroniamelanocarpabsabindingbyspectroscopicstudies
_version_ 1725878653754015744