Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.

<h4>Background</h4>Bovine serum albumin (BSA) contains high affinity binding sites for several endogenous and exogenous compounds and has been used to replace human serum albumin (HSA), as these two compounds share a similar structure. Naringin palmitate is a modified product of naringin...

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Autores principales:	Xia Zhang, Lin Li, Zhenbo Xu, Zhili Liang, Jianyu Su, Jianrong Huang, Bing Li
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6bf54b2ab9334f3ba591bbf21dc82431
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spelling	oai:doaj.org-article:6bf54b2ab9334f3ba591bbf21dc824312021-11-18T07:52:41ZInvestigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.1932-620310.1371/journal.pone.0059106https://doaj.org/article/6bf54b2ab9334f3ba591bbf21dc824312013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23527100/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Bovine serum albumin (BSA) contains high affinity binding sites for several endogenous and exogenous compounds and has been used to replace human serum albumin (HSA), as these two compounds share a similar structure. Naringin palmitate is a modified product of naringin that is produced by an acylation reaction with palmitic acid, which is considered to be an effective substance for enhancing naringin lipophilicity. In this study, the interaction of naringin palmitate with BSA was characterised by spectroscopic and molecular docking techniques.<h4>Methodology/principal findings</h4>The goal of this study was to investigate the interactions between naringin palmitate and BSA under physiological conditions, and differences in naringin and naringin palmitate affinities for BSA were further compared and analysed. The formation of naringin palmitate-BSA was revealed by fluorescence quenching, and the Stern-Volmer quenching constant (KSV ) was found to decrease with increasing temperature, suggesting that a static quenching mechanism was involved. The changes in enthalpy (ΔH) and entropy (ΔS) for the interaction were detected at -4.11 ± 0.18 kJ·mol(-1) and -76.59 ± 0.32 J·mol(-1)·K(-1), respectively, which indicated that the naringin palmitate-BSA interaction occurred mainly through van der Waals forces and hydrogen bond formation. The negative free energy change (ΔG) values of naringin palmitate at different temperatures suggested a spontaneous interaction. Circular dichroism studies revealed that the α-helical content of BSA decreased after interacting with naringin palmitate. Displacement studies suggested that naringin palmitate was partially bound to site I (subdomain IIA) of the BSA, which was also substantiated by the molecular docking studies.<h4>Conclusions/significance</h4>In conclusion, naringin palmitate was transported by BSA and was easily removed afterwards. As a consequence, an extension of naringin applications for use in food, cosmetic and medicinal preparations may be clinically and practically significant, especially in the design of new naringin palmitate-inspired drugs.Xia ZhangLin LiZhenbo XuZhili LiangJianyu SuJianrong HuangBing LiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 3, p e59106 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Xia Zhang Lin Li Zhenbo Xu Zhili Liang Jianyu Su Jianrong Huang Bing Li Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.
description	<h4>Background</h4>Bovine serum albumin (BSA) contains high affinity binding sites for several endogenous and exogenous compounds and has been used to replace human serum albumin (HSA), as these two compounds share a similar structure. Naringin palmitate is a modified product of naringin that is produced by an acylation reaction with palmitic acid, which is considered to be an effective substance for enhancing naringin lipophilicity. In this study, the interaction of naringin palmitate with BSA was characterised by spectroscopic and molecular docking techniques.<h4>Methodology/principal findings</h4>The goal of this study was to investigate the interactions between naringin palmitate and BSA under physiological conditions, and differences in naringin and naringin palmitate affinities for BSA were further compared and analysed. The formation of naringin palmitate-BSA was revealed by fluorescence quenching, and the Stern-Volmer quenching constant (KSV ) was found to decrease with increasing temperature, suggesting that a static quenching mechanism was involved. The changes in enthalpy (ΔH) and entropy (ΔS) for the interaction were detected at -4.11 ± 0.18 kJ·mol(-1) and -76.59 ± 0.32 J·mol(-1)·K(-1), respectively, which indicated that the naringin palmitate-BSA interaction occurred mainly through van der Waals forces and hydrogen bond formation. The negative free energy change (ΔG) values of naringin palmitate at different temperatures suggested a spontaneous interaction. Circular dichroism studies revealed that the α-helical content of BSA decreased after interacting with naringin palmitate. Displacement studies suggested that naringin palmitate was partially bound to site I (subdomain IIA) of the BSA, which was also substantiated by the molecular docking studies.<h4>Conclusions/significance</h4>In conclusion, naringin palmitate was transported by BSA and was easily removed afterwards. As a consequence, an extension of naringin applications for use in food, cosmetic and medicinal preparations may be clinically and practically significant, especially in the design of new naringin palmitate-inspired drugs.
format	article
author	Xia Zhang Lin Li Zhenbo Xu Zhili Liang Jianyu Su Jianrong Huang Bing Li
author_facet	Xia Zhang Lin Li Zhenbo Xu Zhili Liang Jianyu Su Jianrong Huang Bing Li
author_sort	Xia Zhang
title	Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.
title_short	Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.
title_full	Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.
title_fullStr	Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.
title_full_unstemmed	Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.
title_sort	investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/6bf54b2ab9334f3ba591bbf21dc82431
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Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.

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