Evidence map›Paper›PMID 41125981›Full record

ArticleThe protein journal2025

Methylglyoxal-Induced Modification of Hen Egg White Lysozyme: Detection of Advanced Glycation End Products by High Resolution Mass Spectrometry.

Sauradipta Banerjee

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Article in The protein journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 author.

Sauradipta BanerjeeSchool of Chemical Sciences, Indian Association for the Cultivation of Sciences, Kolkata, 700032, India. dipta.saura@gmail.com.

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6 · The paper itself

Abstract

Methylglyoxal is a highly reactive α-oxoaldehyde that forms advanced glycation end products (AGEs) on reaction with proteins. Here, we have studied the effect of methylglyoxal on hen egg white lysozyme (HEWL), after incubation for different time periods (7, 14 and 21 days). Modification with methylglyoxal induced a gradual lowering of tryptophan fluorescence of the protein associated with a blue shift in the wavelength of fluorescence maximum intensity, as observed from tryptophan fluorescence spectra. Secondary structural analysis by far-UV CD spectroscopy indicated a gradual increase in α-helical content of the protein following incubation with methylglyoxal for different time periods. Subsequent analysis of methylglyoxal incubated protein samples using high-resolution ESI-MS, indicated modification of HEWL and formation of AGE adducts. HEWL incubated with methylglyoxal for 7 days indicated the formation of the AGE hydroimidazolone. Several AGE adducts, namely, hydroimidazolone, argpyrimidine, tetrahydropyrimidine, carboxymethyllysine and pyrrolidone-carboxymethyllyine were identified for HEWL incubated with methylglyoxal for 14 days. Thus, the extent of AGE formation was found to increase with increasing period of incubation with the α-oxoaldehyde as revealed by mass spectral analysis. As indicated in further studies, methylglyoxal modification was found to afford considerable resistance to the protein against stress induced aggregation. Considering the high reactivity of the α-dicarbonyl compound, the current study appears worthwhile in terms of detection of methylglyoxal-derived AGE adducts as well as understanding AGE induced protein modifications with clinical implications in treating AGE related disorders.

Indexed as

Glycation End Products, AdvancedMuramidasePyruvaldehydeAnimalsChickensSpectrometry, Mass, Electrospray IonizationGlycation End Products, Advancedhen egg lysozymeMuramidasePyruvaldehydeAdvanced glycation end productsHen egg white lysozymeMaillard reactionMass spectrometryMethylglyoxal

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.