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

(E-pub Ahead of Print)

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

Journal Name: Current Proteomics

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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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Article Details

Published on: 23 April, 2021
(E-pub Ahead of Print)
DOI: 10.2174/1570164618666210423131625
Price: $95

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