ArticleMolecular and cellular biochemistry2010
Non-enzymatic glycation induces structural modifications of myoglobin.
Article in Molecular and cellular biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 44 citations in OpenAlex.
- Major heme proteins hemoglobin and myoglobin with respect to their roles in oxidative stress - a brief review.Frontiers in chemistry · 2025Review
- An overview on glycation: molecular mechanisms, impact on proteins, pathogenesis, and inhibition.Biophysical reviews · 2024Review
- Elevated plasma myoglobin level is closely associated with type 2 diabetic kidney disease.Journal of diabetes · 2024Article
- Vascular nitric oxide resistance in type 2 diabetes.Cell death & disease · 2023Review
- Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose.Molecules (Basel, Switzerland) · 2021Article
- Aqueous solution interactions with sex hormone-binding globulin and estradiol: a theoretical investigation.Journal of biological physics · 2018Article
- Attenuation of Glucose-Induced Myoglobin Glycation and the Formation of Advanced Glycation End Products (AGEs) by (R)-α-Lipoic Acid In Vitro.Biomolecules · 2018Article
- (R)-α-Lipoic acid inhibits fructose-induced myoglobin fructation and the formation of advanced glycation end products (AGEs) in vitro.BMC complementary and alternative medicine · 2018Article
- Formation of Pentosidine Cross-Linking in Myoglobin by Glyoxal: Detection of Fluorescent Advanced Glycation End Product.Journal of fluorescence · 2017Article
- Structural stability of myoglobin and glycomyoglobin: a comparative molecular dynamics simulation study.Journal of biological physics · 2015Article
- Structural and functional alterations of myoglobin by glucose-protein interactions.Journal of molecular modeling · 2014Article
- Effect of non-enzymatic glycation on cystatin: a spectroscopic study.Journal of fluorescence · 2014Article
- In vitro study on structural alteration of myoglobin by methylglyoxal.The protein journal · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Increased glucose concentration in diabetes mellitus causes glycation of several proteins, leading to changes in their properties. Although glycation-induced functional modification of myoglobin is known, structural modification of the protein has not yet been reported. Here, we have studied glucose-modified structural changes of the heme protein. After in vitro glycation of metmyoglobin (Mb) by glucose at 25 degrees C for 6 days, glycated myoglobin (GMb) and unchanged Mb have been separated by ion exchange (BioRex 70) chromatography, and their properties have been compared. Compared to Mb, GMb exhibits increased absorbance around 280 nm and enhanced fluorescence emission with excitation at 285 nm. Fluorescence quenching experiments of the proteins by acrylamide and KI indicate that more surface accessible tryptophan residues are exposed in GMb. CD spectroscopic study reveals a change in the secondary structure of GMb with decreased alpha-helix content. 1-anilino-naphthaline-8-sulfonate (ANS) binding with Mb and GMb indicates that glycation increases hydrophobicity of the heme protein. GMb appears to be less stable with respect to thermal denaturation and differential calorimetry experiments. Heme-globin linkage becomes weaker in GMb, as shown by spectroscopic and gel electrophoresis experiments. A correlation between glycation-induced structural and functional modifications of the heme protein has been suggested.
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