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Mendeleev Communications, 2018, Volume 28, Issue 3, Pages 314–316
DOI: https://doi.org/10.1016/j.mencom.2018.05.029
(Mi mendc1750)
 

This article is cited in 4 scientific papers (total in 4 papers)

Communications

Methylglyoxal modification hinders amyloid conversion of prion protein

S. S. Kudryavtsevaa, A. K. Melnikovabc, V. I. Muronetzc, Yu. Yu. Stroylovacd

a Department of Biology, M.V. Lomonosov Moscow State University, Moscow, Russian Federation
b Department of Bioengineering and Bioinformatics, M.V. Lomonosov Moscow State University, Moscow, Russian Federation
c A.N. Belozersky Research Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russian Federation
d Institute of Molecular Medicine, I.M. Sechenov First Moscow State Medical University, Moscow, Russian Federation
Full-text PDF (529 kB) Citations (4)
Abstract: Effect of glycation by methylglyoxal on prion protein (PrP) structure and properties was evaluated. Modification of arginine at 27-position into a hydroimidazolone derivative was confirmed by MALDI-TOF mass spectrometry; circular dichroism spectra and tryptophan fluorescence showed some structural changes, while the hydrodynamic diameter of PrP was not affected by glycation. Glycated PrP formed large amorphous aggregates instead of intermediate oligomers; seeding of glycated PrP by mature fibrils led to a decreased formation of amyloid structures.
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Document Type: Article
Language: English


Citation: S. S. Kudryavtseva, A. K. Melnikova, V. I. Muronetz, Yu. Yu. Stroylova, “Methylglyoxal modification hinders amyloid conversion of prion protein”, Mendeleev Commun., 28:3 (2018), 314–316
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  • This publication is cited in the following 4 articles:
    Citing articles in Google Scholar: Russian citations, English citations
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