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Formation of Pentosidine Cross-Linking in Myoglobin by Glyoxal: Detection of Fluorescent Advanced Glycation End Product

Banerjee, Sauradipta (2017) Formation of Pentosidine Cross-Linking in Myoglobin by Glyoxal: Detection of Fluorescent Advanced Glycation End Product. In: JOURNAL OF FLUORESCENCE, 27 (4). pp. 1213-1219.

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Official URL: http://dx.doi.org/10.1007/s10895-017-2064-8

Abstract

Glyoxal, a reactive alpha-oxoaldehyde, increases in diabetic condition and reacts with proteins to form advanced glycation end products (AGEs) following Maillard-like reaction. Considering the significance of protein modification by glyoxal-derived AGEs, we investigated the in vitro effect of glyoxal (200 mu M) on the monomeric heme protein myoglobin (Mb) (100 mu M) after incubation for one week at 25 A degrees C. Glyoxal-treated Mb exhibited increased absorbance around the Soret region, decreased alpha-helicity and thermal stability compared to control Mb. Intrinsic fluorescence spectrum of the treated Mb showed an additional signal in the 400-500 nm region on excitation at 280 nm that was absent in control Mb. When excited at 335 nm, the glyoxal-treated sample gave a strong fluorescence indicating AGE formation. Mass spectrometric studies revealed formation of glyoxal-derived fluorescent AGE adduct pentosidine between Lys-145 and Arg-139 residues of Mb. Other than pentosidine, additional AGE adducts, namely, carboxymethyllysine at Lys-133, hydroimidazolone at Arg-31 and pyrrolidone-carboxymethyllysine at Lys-145 were also detected. Lys-145 was thus found to contain two different types of AGE adducts, indicating the heterogeneous nature of in vitro glycation reaction. AGE-induced protein modifications might be associated with complications in disease conditions.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the SPRINGER/PLENUM PUBLISHERS, 233 SPRING ST, NEW YORK, NY 10013 USA
Department/Centre: Division of Mechanical Sciences > Materials Engineering (formerly Metallurgy)
Depositing User: Id for Latest eprints
Date Deposited: 01 Oct 2018 14:13
Last Modified: 01 Oct 2018 14:13
URI: http://eprints.iisc.ac.in/id/eprint/60778

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