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Methylglyoxal modification hinders amyloid conversion of prion protein

Sofia Stanislavovna Kudryavtseva 1
Sofia Stanislavovna Kudryavtseva
, 
Aleksandra Kirillovna Melnikova 2, 3
Aleksandra Kirillovna Melnikova
, 
Vladimir Izrailevich Muronetz 3
Vladimir Izrailevich Muronetz
, 
Yulia Yur'evna Stroylova 3, 4
Yulia Yur'evna Stroylova
10.1016/j.mencom.2018.05.029
Published 2018-04-27
Communication , Volume 28, Issue 3, 314-316
4
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Kudryavtseva S. S. et al. Methylglyoxal modification hinders amyloid conversion of prion protein // Mendeleev Communications. 2018. Vol. 28. No. 3. pp. 314-316.
GOST all authors (up to 50) Copy
Kudryavtseva S. S., Melnikova A. K., Muronetz V. I., Stroylova Y. Y. Methylglyoxal modification hinders amyloid conversion of prion protein // Mendeleev Communications. 2018. Vol. 28. No. 3. pp. 314-316.
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TY - JOUR
DO - 10.1016/j.mencom.2018.05.029
UR - https://mendcomm.colab.ws/publications/10.1016/j.mencom.2018.05.029
TI - Methylglyoxal modification hinders amyloid conversion of prion protein
T2 - Mendeleev Communications
AU - Kudryavtseva, Sofia Stanislavovna
AU - Melnikova, Aleksandra Kirillovna
AU - Muronetz, Vladimir Izrailevich
AU - Stroylova, Yulia Yur'evna
PY - 2018
DA - 2018/04/27
PB - Mendeleev Communications
SP - 314-316
IS - 3
VL - 28
ER -
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@article{2018_Kudryavtseva,
author = {Sofia Stanislavovna Kudryavtseva and Aleksandra Kirillovna Melnikova and Vladimir Izrailevich Muronetz and Yulia Yur'evna Stroylova},
title = {Methylglyoxal modification hinders amyloid conversion of prion protein},
journal = {Mendeleev Communications},
year = {2018},
volume = {28},
publisher = {Mendeleev Communications},
month = {Apr},
url = {https://mendcomm.colab.ws/publications/10.1016/j.mencom.2018.05.029},
number = {3},
pages = {314--316},
doi = {10.1016/j.mencom.2018.05.029}
}
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Kudryavtseva, Sofia Stanislavovna, et al. “Methylglyoxal modification hinders amyloid conversion of prion protein.” Mendeleev Communications, vol. 28, no. 3, Apr. 2018, pp. 314-316. https://mendcomm.colab.ws/publications/10.1016/j.mencom.2018.05.029.

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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