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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doaj-ed1aa325833a4a6a80f15bb1ac72cd522021-10-03T07:42:28ZengDe GruyterOpen Chemistry2391-54202021-09-0119198799710.1515/chem-2021-0089Investigation of bovine serum albumin aggregation upon exposure to silver(i) and copper(ii) metal ions using ZetasizerAlhazmi Hassan A.0Ahsan Waquar1Ibrahim Angum M. M.2Khubrani Rawan Ali Yahya3Haddadi Zainab Ali Abdullah4Safhi Amjad Yahya Fathi5Shubayr Nasser6Al Bratty Mohammed7Najmi Asim8Department of Pharmaceutical Chemistry, College of Pharmacy, Jazan University, P.O. Box 114, Jazan, Saudi ArabiaDepartment of Pharmaceutical Chemistry, College of Pharmacy, Jazan University, P.O. Box 114, Jazan, Saudi ArabiaDepartment of Pharmaceutical Chemistry, College of Pharmacy, Jazan University, P.O. Box 114, Jazan, Saudi ArabiaCollege of Pharmacy, Jazan University, P.O. Box 114, Jazan, Saudi ArabiaCollege of Pharmacy, Jazan University, P.O. Box 114, Jazan, Saudi ArabiaCollege of Pharmacy, Jazan University, P.O. Box 114, Jazan, Saudi ArabiaDiagnostic Radiology Department, College of Applied Medical Sciences, Jazan University, P.O. Box No. 114, Jazan, Saudi ArabiaDepartment of Pharmaceutical Chemistry, College of Pharmacy, Jazan University, P.O. Box 114, Jazan, Saudi ArabiaDepartment of Pharmaceutical Chemistry, College of Pharmacy, Jazan University, P.O. Box 114, Jazan, Saudi ArabiaDepending 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.https://doi.org/10.1515/chem-2021-0089coppersilvermetal ionsbsaaggregationzetasizer |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
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 |
spellingShingle |
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 Open Chemistry copper silver metal ions bsa aggregation zetasizer |
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 |
series |
Open Chemistry |
issn |
2391-5420 |
publishDate |
2021-09-01 |
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. |
topic |
copper silver metal ions bsa aggregation zetasizer |
url |
https://doi.org/10.1515/chem-2021-0089 |
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