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Rapid myoglobin aggregation through glucosamine-induced α-dicarbonyl formation Open Access

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Author or creator
Hrynets, Yuliya
Ndagijimana, Maurice
Betti, Mirko
Additional contributors
Subject/Keyword
Heme
Electrospray Ionization Mass Spectrometry
Chemical Precipitation
Protein Structure
Fluorescence
Maillard Reaction
Oxidation
Glycation
Type of item
Journal Article (Published)
Language
English
Place
Time
Description
The extent of glycation and conformational changes of horse myoglobin (Mb) upon glycation with N-acetyl-glucosamine (GlcNAc), glucose (Glc) and glucosamine (GlcN) were investigated. Among tested sugars, the rate of glycation with GlcN was the most rapid as shown by MALDI and ESI mass spectrometries. Protein oxidation, as evaluated by the amount of carbonyl groups present on Mb, was found to increase exponentially in Mb-Glc conjugates over time, whereas in Mb-GlcN mixtures the carbonyl groups decreased significantly after maximum at 3 days of the reaction. The reaction between GlcN and Mb resulted in a significantly higher amount of α-dicarbonyl compounds, mostly glucosone and 3-deoxyglucosone, ranging from and 27 to 332 mg/L and from 14 to 304 mg/L, respectively. Already at 0.5 days, tertiary structural changes of Mb-GlcN conjugate were observed by altered tryptophan fluorescence. A reduction of metmyoglobin to deoxy-and oxymyoglobin forms was observed on the first day of reaction, coinciding with the greatest amount of glucosone produced. In contrast to native α-helical myoglobin, 41% of the glycated protein sequence was transformed into a β-sheet conformation, as determined by circular dichroism spectropolarimetry. Transmission electron microscopy demonstrated that Mb glycation with GlcN causes the formation of amorphous or fibrous aggregates, started already at 3 reaction days. These aggregates bind to an amyloid-specific dye thioflavin T. With the aid of α-dicarbonyl compounds and advanced products of reaction, this study suggests that the Mb glycation with GlcN induces the unfolding of an initially globular protein structure into amyloid fibrils comprised of a β-sheet structure.
Date created
2015
DOI
doi:10.7939/R30G3HB8C
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Hrynets, Y., Ndagijimana, M., & Betti, M. (2015). Rapid myoglobin aggregation through glucosamine-induced α-dicarbonyl formation. PLoS ONE, 10(9), e0139022 [23 pages].  http://dx.doi.org/10.1371/journal.pone.0139022

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File title: Rapid Myoglobin Aggregation through Glucosamine-Induced α-Dicarbonyl Formation
File title: Rapid Myoglobin Aggregation through Glucosamine-Induced -Dicarbonyl Formation
File author: Yuliya Hrynets, Maurice Ndagijimana, Mirko Betti
Page count: 23
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