STUDIES ON THE INTERACTION BETWEEN TRIPTOLIDE AND BOVINE SERUM ALBUMIN (BSA) BY SPECTROSCOPIC AND MOLECULAR MODELING METHODS
BACKGROUND: Triptolide is a major active constituent isolated from Tripterygiumwilfordii Hook F, a Chinese herbal medicine. This study investigated the intermolecular interaction between triptolide and bovine serum albumin (BSA). MATERIALS AND METHODS: The fluorescence, circular dichroism (CD) and m...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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African Traditional Herbal Medicine Supporters Initiative (ATHMSI)
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5412182/ https://www.ncbi.nlm.nih.gov/pubmed/28480368 http://dx.doi.org/10.21010/ajtcam.v13i6.17 |
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author | Wang, Haidong Shi, Hailang Pang, Jie Song, Xingfa Xu, Caiyun Sun, Zengxian |
author_facet | Wang, Haidong Shi, Hailang Pang, Jie Song, Xingfa Xu, Caiyun Sun, Zengxian |
author_sort | Wang, Haidong |
collection | PubMed |
description | BACKGROUND: Triptolide is a major active constituent isolated from Tripterygiumwilfordii Hook F, a Chinese herbal medicine. This study investigated the intermolecular interaction between triptolide and bovine serum albumin (BSA). MATERIALS AND METHODS: The fluorescence, circular dichroism (CD) and molecular docking methods were used to investigate the intermolecular interaction between triptolide and BSA. The binding constant, the number of binding sites, binding subdomain and the thermodynamic parameters were measured. RESULTS: The results of this experiment revealed that the intrinsic fluorescence of BSA was effectively quenched by triptolide via static quenching. The experimental results of synchronous fluorescence and CD spectra showed that the conformation of BSA was changed in the presence of triptolide. CONCLUSION: It indicated that triptolide could spontaneously bind on site II (subdomain IIIA) of BSA mainly via hydrogen bonding interactions and Van der Waals force. |
format | Online Article Text |
id | pubmed-5412182 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | African Traditional Herbal Medicine Supporters Initiative (ATHMSI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-54121822017-09-29 STUDIES ON THE INTERACTION BETWEEN TRIPTOLIDE AND BOVINE SERUM ALBUMIN (BSA) BY SPECTROSCOPIC AND MOLECULAR MODELING METHODS Wang, Haidong Shi, Hailang Pang, Jie Song, Xingfa Xu, Caiyun Sun, Zengxian Afr J Tradit Complement Altern Med Article BACKGROUND: Triptolide is a major active constituent isolated from Tripterygiumwilfordii Hook F, a Chinese herbal medicine. This study investigated the intermolecular interaction between triptolide and bovine serum albumin (BSA). MATERIALS AND METHODS: The fluorescence, circular dichroism (CD) and molecular docking methods were used to investigate the intermolecular interaction between triptolide and BSA. The binding constant, the number of binding sites, binding subdomain and the thermodynamic parameters were measured. RESULTS: The results of this experiment revealed that the intrinsic fluorescence of BSA was effectively quenched by triptolide via static quenching. The experimental results of synchronous fluorescence and CD spectra showed that the conformation of BSA was changed in the presence of triptolide. CONCLUSION: It indicated that triptolide could spontaneously bind on site II (subdomain IIIA) of BSA mainly via hydrogen bonding interactions and Van der Waals force. African Traditional Herbal Medicine Supporters Initiative (ATHMSI) 2016-09-29 /pmc/articles/PMC5412182/ /pubmed/28480368 http://dx.doi.org/10.21010/ajtcam.v13i6.17 Text en Copyright: © 2016 Afr. J. Traditional Complementary and Alternative Medicines http://creativecommons.org/licenses/CC-BY/4.0 This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License |
spellingShingle | Article Wang, Haidong Shi, Hailang Pang, Jie Song, Xingfa Xu, Caiyun Sun, Zengxian STUDIES ON THE INTERACTION BETWEEN TRIPTOLIDE AND BOVINE SERUM ALBUMIN (BSA) BY SPECTROSCOPIC AND MOLECULAR MODELING METHODS |
title | STUDIES ON THE INTERACTION BETWEEN TRIPTOLIDE AND BOVINE SERUM ALBUMIN (BSA) BY SPECTROSCOPIC AND MOLECULAR MODELING METHODS |
title_full | STUDIES ON THE INTERACTION BETWEEN TRIPTOLIDE AND BOVINE SERUM ALBUMIN (BSA) BY SPECTROSCOPIC AND MOLECULAR MODELING METHODS |
title_fullStr | STUDIES ON THE INTERACTION BETWEEN TRIPTOLIDE AND BOVINE SERUM ALBUMIN (BSA) BY SPECTROSCOPIC AND MOLECULAR MODELING METHODS |
title_full_unstemmed | STUDIES ON THE INTERACTION BETWEEN TRIPTOLIDE AND BOVINE SERUM ALBUMIN (BSA) BY SPECTROSCOPIC AND MOLECULAR MODELING METHODS |
title_short | STUDIES ON THE INTERACTION BETWEEN TRIPTOLIDE AND BOVINE SERUM ALBUMIN (BSA) BY SPECTROSCOPIC AND MOLECULAR MODELING METHODS |
title_sort | studies on the interaction between triptolide and bovine serum albumin (bsa) by spectroscopic and molecular modeling methods |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5412182/ https://www.ncbi.nlm.nih.gov/pubmed/28480368 http://dx.doi.org/10.21010/ajtcam.v13i6.17 |
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