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.
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
Linking options:
https://www.mathnet.ru/eng/mendc1750
https://www.mathnet.ru/eng/mendc/v28/i3/p314
This publication is cited in the following 3 articles:
Vladimir I. Muronets, Sofiya S. Kudryavtseva, Lidia P. Kurochkina, Evgeniia V. Leisi, Yulia Yu. Stroylova, Elena V. Schmalhausen, “Factors Affecting Pathological Amyloid Protein Transformation: From Post-Translational Modifications to Chaperones”, Biochemistry Moscow, 90:S1 (2025), S164
Qian Wu, Yinggang Liang, Yingfei Kong, Fen Zhang, Yingna Feng, Yu Ouyang, Chao Wang, Zhiqiang Guo, Juan Xiao, Nianjie Feng, “Role of glycated proteins in vivo: Enzymatic glycated proteins and non-enzymatic glycated proteins”, Food Research International, 155 (2022), 111099
S.S. Kudryavtseva, Y.Y. Stroylova, L.P. Kurochkina, V.I. Muronetz, “The chaperonin TRiC is blocked by native and glycated prion protein”, Archives of Biochemistry and Biophysics, 683 (2020), 108319