Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb(III) and Sb(V).

Antimony is a metalloid that affects biological functions in humans due to a mechanism still not understood. There is no doubt that the toxicity and physicochemical properties of Sb are strongly related with its chemical state. In this paper, the interaction between Sb(III) and Sb(V) with bovine ser...

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Main Authors: Marcelo Verdugo, Jorge Ruiz Encinar, José Manuel Costa-Fernández, Mario Menendez-Miranda, Diego Bouzas-Ramos, Manuel Bravo, Waldo Quiroz
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2017-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC5289473?pdf=render
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spelling doaj-d9b0d36f29654a36965f3f683d0183d02020-11-25T02:23:37ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01122e017086910.1371/journal.pone.0170869Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb(III) and Sb(V).Marcelo VerdugoJorge Ruiz EncinarJosé Manuel Costa-FernándezMario Menendez-MirandaDiego Bouzas-RamosManuel BravoWaldo QuirozAntimony is a metalloid that affects biological functions in humans due to a mechanism still not understood. There is no doubt that the toxicity and physicochemical properties of Sb are strongly related with its chemical state. In this paper, the interaction between Sb(III) and Sb(V) with bovine serum albumin (BSA) was investigated in vitro by fluorescence spectroscopy, and circular dichroism (CD) under simulated physiological conditions. Moreover, the coupling of the separation technique, asymmetric flow field-flow fractionation, with elemental mass spectrometry to understand the interaction of Sb(V) and Sb(III) with the BSA was also used. Our results showed a different behaviour of Sb(III) vs. Sb(V) regarding their effects on the interaction with the BSA. The effects in terms of protein aggregates and conformational changes were higher in the presence of Sb(III) compared to Sb(V) which may explain the differences in toxicity between both Sb species in vivo. Obtained results demonstrated the protective effect of GSH that modifies the degree of interaction between the Sb species with BSA. Interestingly, in our experiments it was possible to detect an interaction between BSA and Sb species, which may be related with the presence of labile complex between the Sb and a protein for the first time.http://europepmc.org/articles/PMC5289473?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Marcelo Verdugo
Jorge Ruiz Encinar
José Manuel Costa-Fernández
Mario Menendez-Miranda
Diego Bouzas-Ramos
Manuel Bravo
Waldo Quiroz
spellingShingle Marcelo Verdugo
Jorge Ruiz Encinar
José Manuel Costa-Fernández
Mario Menendez-Miranda
Diego Bouzas-Ramos
Manuel Bravo
Waldo Quiroz
Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb(III) and Sb(V).
PLoS ONE
author_facet Marcelo Verdugo
Jorge Ruiz Encinar
José Manuel Costa-Fernández
Mario Menendez-Miranda
Diego Bouzas-Ramos
Manuel Bravo
Waldo Quiroz
author_sort Marcelo Verdugo
title Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb(III) and Sb(V).
title_short Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb(III) and Sb(V).
title_full Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb(III) and Sb(V).
title_fullStr Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb(III) and Sb(V).
title_full_unstemmed Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb(III) and Sb(V).
title_sort study of conformational changes and protein aggregation of bovine serum albumin in presence of sb(iii) and sb(v).
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2017-01-01
description Antimony is a metalloid that affects biological functions in humans due to a mechanism still not understood. There is no doubt that the toxicity and physicochemical properties of Sb are strongly related with its chemical state. In this paper, the interaction between Sb(III) and Sb(V) with bovine serum albumin (BSA) was investigated in vitro by fluorescence spectroscopy, and circular dichroism (CD) under simulated physiological conditions. Moreover, the coupling of the separation technique, asymmetric flow field-flow fractionation, with elemental mass spectrometry to understand the interaction of Sb(V) and Sb(III) with the BSA was also used. Our results showed a different behaviour of Sb(III) vs. Sb(V) regarding their effects on the interaction with the BSA. The effects in terms of protein aggregates and conformational changes were higher in the presence of Sb(III) compared to Sb(V) which may explain the differences in toxicity between both Sb species in vivo. Obtained results demonstrated the protective effect of GSH that modifies the degree of interaction between the Sb species with BSA. Interestingly, in our experiments it was possible to detect an interaction between BSA and Sb species, which may be related with the presence of labile complex between the Sb and a protein for the first time.
url http://europepmc.org/articles/PMC5289473?pdf=render
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