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

Hassan A Alhazmi,Asim Najmi,Rawan Ali Yahya Khubrani,Nasser Shubayr,Zainab Ali Abdullah Haddadi,Amjad Yahya Fathi Safhi,Waquar Ahsan,Mohammed Al Bratty,Angum M M Ibrahim

doi:10.1515/chem-2021-0089

Hassan A Alhazmi, Asim Najmi + Show 7 more

Open Access

https://doi.org/10.1515/chem-2021-0089

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Journal: Open chemistry	Publication Date: Sep 24, 2021
Citations: 5	License type: CC BY 4.0

Affiliation: Jazan University

Abstract

Abstract 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.

Highlights

Copper (Cu) and Silver (Ag) are closely resembled coinage metals grouped together in group 11 and are being used for centuries as antimicrobial agents in healthcare systems and agriculture
The size of bovine serum albumin (BSA) protein at 10 μM concentration was measured in the tris HCl buffer and was found to be of 13.18 nm (87.5%) with a zeta potential of −15.5 mV, which showed that the BSA molecules were present in the normal size corresponding to the native protein and were segregated in the solution
The instrument was sensitive in detecting the size and zeta potential of the protein molecules and gave a preliminary idea about the metal-concentration and time at which the protein aggregation could take place in biological systems

Summary

Introduction

Copper (Cu) and Silver (Ag) are closely resembled coinage metals grouped together in group 11 and are being used for centuries as antimicrobial agents in healthcare systems and agriculture. These ions are shown to bind to important molecules, leading to disruption of their function [1] Exposure to these metal ions often occurs via skin contact and inside the human body; these metal ions bind to various macromolecules including proteins inducing structural changes and aggregation which may result in health hazards. These metal ions upon reaching the systemic circulation interact with plasma proteins leading to aggregation of proteins and increase in the coefficient of friction, thereby influencing the biointerface reactions.

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