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...
Main Authors: | , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
SpringerOpen
2018-05-01
|
Series: | AMB Express |
Subjects: | |
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 |