Methylglyoxal modification hinders amyloid conversion of prion protein
Kudryavtseva S. S., Melnikova A. K., Muronetz V. I., Strojlova Yu. Yu.
Mendeleev Communications
Vol.28, Issue3, P. 314-316
Опубликовано: 2018
Тип ресурса: Статья
DOI:10.1016/j.mencom.2018.05.029
Аннотация:
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. © 2018
Язык текста: Английский
ISSN: 1364-551X
Kudryavtseva S. S.
Melnikova A. K.
Muronetz V. I.
Strojlova Yu. Yu. Yuliya Yuryevna 1984-
Кудрявцева С. С.
Мелникова А. К.
Муронетз В. И.
Стройлова Ю. Ю. Юлия Юрьевна 1984-
Methylglyoxal modification hinders amyloid conversion of prion protein
Текст визуальный непосредственный
Mendeleev Communications
Elsevier Science Publisher B.V.
Vol.28, Issue3 P. 314-316
2018
Статья
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. © 2018