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Investigation of the interaction between two phenylethanoid glycosides and bovine serum albumin by spectroscopic methods

Two phenylethanoid glycosides, acteoside and forsythoside B, were first isolated from the traditional Chinese herb Callicarpa peii H.T. Chang. The interaction between the two phenylethanoid glycosides and bovine serum albumin (BSA) was investigated by fluorescence, UV–vis absorbance and circular dic...

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Detalles Bibliográficos
Autores principales: Wu, Ai-Zhi, Lin, Chao-Zhan, Zhai, Ya-Jing, Zhuo, Jia-Lin, Zhu, Chen-Chen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Xi'an Jiaotong University 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5760947/
https://www.ncbi.nlm.nih.gov/pubmed/29403797
http://dx.doi.org/10.1016/j.jpha.2012.07.001
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author Wu, Ai-Zhi
Lin, Chao-Zhan
Zhai, Ya-Jing
Zhuo, Jia-Lin
Zhu, Chen-Chen
author_facet Wu, Ai-Zhi
Lin, Chao-Zhan
Zhai, Ya-Jing
Zhuo, Jia-Lin
Zhu, Chen-Chen
author_sort Wu, Ai-Zhi
collection PubMed
description Two phenylethanoid glycosides, acteoside and forsythoside B, were first isolated from the traditional Chinese herb Callicarpa peii H.T. Chang. The interaction between the two phenylethanoid glycosides and bovine serum albumin (BSA) was investigated by fluorescence, UV–vis absorbance and circular dichroism (CD). The results showed that the quenching mechanism in the drug–BSA binary systems was a combination of static quenching and non-radiative energy transfer. Displacement experiments confirmed that the drug bound to the site I of BSA. UV–vis and CD measurements indicated that the binding of the drug to BSA induced conformational changes in BSA.
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spelling pubmed-57609472018-02-05 Investigation of the interaction between two phenylethanoid glycosides and bovine serum albumin by spectroscopic methods Wu, Ai-Zhi Lin, Chao-Zhan Zhai, Ya-Jing Zhuo, Jia-Lin Zhu, Chen-Chen J Pharm Anal Article Two phenylethanoid glycosides, acteoside and forsythoside B, were first isolated from the traditional Chinese herb Callicarpa peii H.T. Chang. The interaction between the two phenylethanoid glycosides and bovine serum albumin (BSA) was investigated by fluorescence, UV–vis absorbance and circular dichroism (CD). The results showed that the quenching mechanism in the drug–BSA binary systems was a combination of static quenching and non-radiative energy transfer. Displacement experiments confirmed that the drug bound to the site I of BSA. UV–vis and CD measurements indicated that the binding of the drug to BSA induced conformational changes in BSA. Xi'an Jiaotong University 2013-02 2012-07-08 /pmc/articles/PMC5760947/ /pubmed/29403797 http://dx.doi.org/10.1016/j.jpha.2012.07.001 Text en © 2012 Xi'an Jiaotong University http://creativecommons.org/licenses/by-nc-nd/3.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).
spellingShingle Article
Wu, Ai-Zhi
Lin, Chao-Zhan
Zhai, Ya-Jing
Zhuo, Jia-Lin
Zhu, Chen-Chen
Investigation of the interaction between two phenylethanoid glycosides and bovine serum albumin by spectroscopic methods
title Investigation of the interaction between two phenylethanoid glycosides and bovine serum albumin by spectroscopic methods
title_full Investigation of the interaction between two phenylethanoid glycosides and bovine serum albumin by spectroscopic methods
title_fullStr Investigation of the interaction between two phenylethanoid glycosides and bovine serum albumin by spectroscopic methods
title_full_unstemmed Investigation of the interaction between two phenylethanoid glycosides and bovine serum albumin by spectroscopic methods
title_short Investigation of the interaction between two phenylethanoid glycosides and bovine serum albumin by spectroscopic methods
title_sort investigation of the interaction between two phenylethanoid glycosides and bovine serum albumin by spectroscopic methods
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5760947/
https://www.ncbi.nlm.nih.gov/pubmed/29403797
http://dx.doi.org/10.1016/j.jpha.2012.07.001
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