Structural changes of human serum albumin in response to a low concentration of heavy ions.

Journal of Biophotonics
Anushree Saha, Vladislav V Yakovlev

Abstract

Lead ions in solution interact strongly with human serum albumin and modify the properties and function of albumin molecules. In the present study, we used optical spectroscopic techniques to explore the binding sites of lead, present in albumin. Structural and chemical analysis of albumin molecules using fluorescence and Raman spectroscopy, predicted the modification of two major amino acids in albumin due to lead binding. No secondary structural changes are observed in the protein molecule, which is further confirmed using circular dichroism absorption measurements. The results indicate that loss of charge from the binding site of albumin by the charged lead ions, give rise to dipole interaction which acts as the major contributor to promote protein agglomeration.

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Citations

Mar 25, 2014·Environmental Toxicology and Pharmacology·Dai ChunmeiZheng Dan
Jul 10, 2016·Lasers in Medical Science·Maurício Liberal de AlmeidaLandulfo Silveira
Jun 30, 2019·Journal of Biophotonics·Chandavalli R RaghushakerKrishna K Mahato
Jul 13, 2019·Photodiagnosis and Photodynamic Therapy·Saranjam KhanIftikhar Ahmad
Feb 5, 2021·Journal of Hazardous Materials·Shanjun SongZongwei Cai

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