Effect of peroxynitrite on human serum albumin: a multi technique approach

Arif, Z. and Arfat, M.Y. and Neelofar, K. and Ahmad, S. and Badar, A. and Khan, M.A. and Zaman, A. and Ahmad, J. (2017) Effect of peroxynitrite on human serum albumin: a multi technique approach. Journal of Biomolecular Structure and Dynamics, 35 (9). pp. 2066-2076. ISSN 7391102

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In this study, human serum albumin (HSA), the most abundant protein of blood plasma, was modified with varying concentrations of peroxynitrite. The peroxynitrite-induced changes in HSA was monitored by spectroscopy, SDS-PAGE, 1-anilinonaphthalene-8-sulfonic acid (ANS), thermal denaturation studies, and matrix-assisted laser desorption/inonization-time of flight mass spectrometry (MALDI-TOF MS). Aggregate formation was studied by thioflavin T binding and scanning electron microscopy (SEM). The results indicated formation of 3-nitrotyrosine, 6-nitrotryptophan, dityrosine, and carbonyls in modified samples and showed retarded mobility in SDS–polyacrylamide gel. Reduction in α-helicity and surface protein hydrophobicity confirmed the secondary and tertiary structure alterations in peroxynitrite-modified-HSA. Also, attachment of nitro group and increase in melting temperature was observed in modified sample. Furthermore, significant enhancement in the fluorescence intensity of ThT upon binding with peroxynitrite-modified-HSA and images under scanning electron microscope are suggestive of protein aggregation. It is, therefore, speculated that HSA modified by endogenously formed peroxynitrite might act as a trigger for nitration/aggregation and suggested the role of peroxynitrite-modified-HSA in SLE.

Item Type: Article
Uncontrolled Keywords: 3-nitrotyrosine; HSA; scanning electron microscopy; SLE
Subjects: R Medicine > R Medicine (General)
Divisions: Faculties > Faculty of Life Sciences > Department of Biochemistry
Depositing User: AMU Library
Date Deposited: 23 Jan 2018 04:41
Last Modified: 23 Jan 2018 04:41
URI: http://ir.amu.ac.in/id/eprint/10909

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