Characterization of methylglyoxal-modified human IgG by physicochemical methods

Khan, M.A. and Arif, Z. and Moinuddin, . and Alam, K. (2017) Characterization of methylglyoxal-modified human IgG by physicochemical methods. Journal of Biomolecular Structure and Dynamics. pp. 1-12. ISSN 7391102

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Human IgG is a defence protein and quite reactive to dicarbonyls. In this study, methylglyoxal-induced modification of IgG was examined by various biochemical and biophysical methods. The methylglyoxal-induced changes in IgG were monitored by UV-visible and fluorescence spectroscopy, Fourier transform infrared spectroscopy, 1-anilinonaphthalene-8-sulfonic acid (ANS), and thermal denaturation studies. Aggregate formation was studied by Thioflavin T (ThT), Congo red (CR) and scanning electron microscopy (SEM) and transmission electron microscopy (TEM). Spectroscopic studies suggested gross changes in MGO-modified IgG. Fluorogenic AGEs appeared during modification and the MGO-modified IgG gained thermostability. The reaction produced oxidative stress in the medium because carbonyl content increased manifold and sulfhydryl groups decreased. Enhanced binding of the MGO-modified IgG by Congo red and Thioflavin T suggests crosslinking and aggregation. This was supported by SEM and TEM results.

Item Type: Article
Uncontrolled Keywords: crosslink; Human IgG; hyperglycemia; methylglyoxal; protein aggregate
Subjects: R Medicine > R Medicine (General)
Divisions: Faculties > Faculty of Life Sciences > Department of Biochemistry
Depositing User: AMU Library
Date Deposited: 22 Jan 2018 10:52
Last Modified: 22 Jan 2018 10:52

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