Investigation of bovine serum albumin aggregation upon exposure to silver(i) and copper(ii) metal ions using Zetasizer

Depending upon the metal coordination capacity and the binding sites of proteins, interaction between metal and proteins leads to a number of changes in the protein molecule which may include the change in conformation, unfolding, overall charge, and aggregation in some cases. In this study, Cu(ii)...

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Autores principales:	Alhazmi Hassan A., Ahsan Waquar, Ibrahim Angum M. M., Khubrani Rawan Ali Yahya, Haddadi Zainab Ali Abdullah, Safhi Amjad Yahya Fathi, Shubayr Nasser, Al Bratty Mohammed, Najmi Asim
Formato:	article
Lenguaje:	EN
Publicado:	De Gruyter 2021
Materias:	copper silver metal ions bsa aggregation zetasizer Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/ed1aa325833a4a6a80f15bb1ac72cd52
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spelling	oai:doaj.org-article:ed1aa325833a4a6a80f15bb1ac72cd522021-12-05T14:10:44ZInvestigation of bovine serum albumin aggregation upon exposure to silver(i) and copper(ii) metal ions using Zetasizer2391-542010.1515/chem-2021-0089https://doaj.org/article/ed1aa325833a4a6a80f15bb1ac72cd522021-09-01T00:00:00Zhttps://doi.org/10.1515/chem-2021-0089https://doaj.org/toc/2391-5420Depending upon the metal coordination capacity and the binding sites of proteins, interaction between metal and proteins leads to a number of changes in the protein molecule which may include the change in conformation, unfolding, overall charge, and aggregation in some cases. In this study, Cu(ii) and Ag(i) metal ions were selected to investigate aggregation of bovine serum albumin (BSA) molecule upon interaction by measuring the size and charge of the aggregates using nano-Zetasizer instrument. Two concentrations of metal ions were made to interact with a specific concentration of BSA and the size and zeta potential of BSA aggregates were measured from 0 min upto 18 h. The Cu(ii) and Ag(i) metal ions showed almost similar behavior in inducing the BSA aggregation and the intensity of peak corresponding to the normal-sized protein decreased with time, whereas the peak corresponding to the protein aggregate increased. However, the effect on zeta potential of the aggregates was observed to be different with both metal ions. The aggregation of protein due to interaction of different metal ions is important to study as it gives insight to the pathogenesis of many neurological disorders and would result in developing effective ways to limit their exposure.Alhazmi Hassan A.Ahsan WaquarIbrahim Angum M. M.Khubrani Rawan Ali YahyaHaddadi Zainab Ali AbdullahSafhi Amjad Yahya FathiShubayr NasserAl Bratty MohammedNajmi AsimDe Gruyterarticlecoppersilvermetal ionsbsaaggregationzetasizerChemistryQD1-999ENOpen Chemistry, Vol 19, Iss 1, Pp 987-997 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	copper silver metal ions bsa aggregation zetasizer Chemistry QD1-999
spellingShingle	copper silver metal ions bsa aggregation zetasizer Chemistry QD1-999 Alhazmi Hassan A. Ahsan Waquar Ibrahim Angum M. M. Khubrani Rawan Ali Yahya Haddadi Zainab Ali Abdullah Safhi Amjad Yahya Fathi Shubayr Nasser Al Bratty Mohammed Najmi Asim Investigation of bovine serum albumin aggregation upon exposure to silver(i) and copper(ii) metal ions using Zetasizer
description	Depending upon the metal coordination capacity and the binding sites of proteins, interaction between metal and proteins leads to a number of changes in the protein molecule which may include the change in conformation, unfolding, overall charge, and aggregation in some cases. In this study, Cu(ii) and Ag(i) metal ions were selected to investigate aggregation of bovine serum albumin (BSA) molecule upon interaction by measuring the size and charge of the aggregates using nano-Zetasizer instrument. Two concentrations of metal ions were made to interact with a specific concentration of BSA and the size and zeta potential of BSA aggregates were measured from 0 min upto 18 h. The Cu(ii) and Ag(i) metal ions showed almost similar behavior in inducing the BSA aggregation and the intensity of peak corresponding to the normal-sized protein decreased with time, whereas the peak corresponding to the protein aggregate increased. However, the effect on zeta potential of the aggregates was observed to be different with both metal ions. The aggregation of protein due to interaction of different metal ions is important to study as it gives insight to the pathogenesis of many neurological disorders and would result in developing effective ways to limit their exposure.
format	article
author	Alhazmi Hassan A. Ahsan Waquar Ibrahim Angum M. M. Khubrani Rawan Ali Yahya Haddadi Zainab Ali Abdullah Safhi Amjad Yahya Fathi Shubayr Nasser Al Bratty Mohammed Najmi Asim
author_facet	Alhazmi Hassan A. Ahsan Waquar Ibrahim Angum M. M. Khubrani Rawan Ali Yahya Haddadi Zainab Ali Abdullah Safhi Amjad Yahya Fathi Shubayr Nasser Al Bratty Mohammed Najmi Asim
author_sort	Alhazmi Hassan A.
title	Investigation of bovine serum albumin aggregation upon exposure to silver(i) and copper(ii) metal ions using Zetasizer
title_short	Investigation of bovine serum albumin aggregation upon exposure to silver(i) and copper(ii) metal ions using Zetasizer
title_full	Investigation of bovine serum albumin aggregation upon exposure to silver(i) and copper(ii) metal ions using Zetasizer
title_fullStr	Investigation of bovine serum albumin aggregation upon exposure to silver(i) and copper(ii) metal ions using Zetasizer
title_full_unstemmed	Investigation of bovine serum albumin aggregation upon exposure to silver(i) and copper(ii) metal ions using Zetasizer
title_sort	investigation of bovine serum albumin aggregation upon exposure to silver(i) and copper(ii) metal ions using zetasizer
publisher	De Gruyter
publishDate	2021
url	https://doaj.org/article/ed1aa325833a4a6a80f15bb1ac72cd52
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Investigation of bovine serum albumin aggregation upon exposure to silver(i) and copper(ii) metal ions using Zetasizer

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