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Current Proteomics

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ISSN (Print): 1570-1646
ISSN (Online): 1875-6247

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Research Article

Arsenite Induced Conformational Changes and Aggregation in Human Serum Albumin (HSA) and its Prevention by Naringin

Author(s): Shamila Fatima, Fareeha Arshad and Samreen Amani*

Volume 19, Issue 2, 2022

Published on: 23 April, 2021

Page: [153 - 162] Pages: 10

DOI: 10.2174/1570164618666210423131625

Price: $65

Abstract

Background: Heavy metals and metalloids like arsenic, cadmium, mercury acts as denaturing agent for biomolecules. They interfere with protein’s physiological activity by forming a complex with the protein’s side chain or removing the essential metal ions from metalloproteins and replacing them. Protein aggregation is an extensive phenomenon in a cell and is linked with various pathological conditions.

Aim: In this study, we aim to prove that proteins are highly susceptible to arsenite toxicity by arsenite-induced protein aggregation; and that naringin reduces the aggregation effect.

Methods: Several biophysical techniques were employed to study the protein aggregation due to arsenite and its prevention by naringin.

Results: Through our experiments, the results showed that aggregation induced by arsenite was reduced in the presence of naringin at twice the concentration of arsenite.

Conclusion: In conclusion, our study showed that naringin plays a protective role during HSA aggregation due to arsenite.

Keywords: Protein aggregation, arsenite, naringin, HSA, amyloid diseases, congo red.

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