Evaluation of structure, chaperone-like activity and protective ability of peroxynitrite modified human α-Crystallin subunits against copper-mediated ascorbic acid oxidation

International Journal of Biological Macromolecules
Maryam GhahramaniBoris I Kurganov

Abstract

The copper-catalyzed oxidation of ascorbic acid (ASA) to dehydroascorbate (DHA) and hydrogen peroxide plays a central role in pathology of cataract diseases during ageing and in diabetic patients. In the current study, the structural feature, chaperone-like activity and protective ability of peroxynitrite (PON) modified αA- and αB-Crystallin (Cry) against copper-mediated ASA oxidation were studied using different spectroscopic measurements and gel mobility shift assay. Upon PON modification, additional to protein structural alteration, the contents of nitrotyrosine, nitrotryptophan, dityrosine and carbonyl groups were significantly increased. Moreover, αB-Cry demonstrates significantly larger capacity for PON modification than αA-Cry. Also, based on the extent of PON modification, these proteins may display an improved chaperone-like activity and enhanced protective ability against copper-mediated ASA oxidation. In the presence of copper ions, chaperone-like activity of both native and PON-modified α-Cry subunits were appreciably improved. Additionally, binding of copper ions to native and PON-modified proteins results in the significant reduction of their solvent exposed hydrophobic patches. Overall, the increase in chaperone-...Continue Reading

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Citations

May 16, 2017·Journal of Biomolecular Structure & Dynamics·Fataneh JafariMohsen Shahlaei
Sep 20, 2019·Cell Biochemistry and Biophysics·Maryam Kianpour, Reza Yousefi
May 18, 2018·Vestnik oftalmologii·S E AvetisovV G Motalov
Jun 19, 2016·International Journal of Biological Macromolecules·Afrooz AnbarakiReza Yousefi

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