Structural features of the ionic self-complementary amyloidogenic peptide

3rd International Conference on Small Angle Neutron Scattering dedicated to the 80 anniversary of Yu.M. Ostanevich

Egorov, V.V.^1,2 ; Zabrodskaya, Ya.A.^2 ; Lebedev, D.V.^1 ; Gorshkov, A.N.^2 ; Kuklin, A.I.^3,4

DMRB PNPI NRC KI, Gatchina, Russia^1

Influenza Institute MH of Russia, Saint-Petersburg, Russia^2

Joint Institute for Nuclear Research, Dubna, Russia^3

Moscow Institute of Physics and Technology, State University, Dolgoprudny, Russia^4

关键词: Amyloid fibril;    Amyloidogenic peptides;    MALDI-mass spectrometry;    Structural feature;   

Others  :  https://iopscience.iop.org/article/10.1088/1742-6596/848/1/012022/pdf
DOI  :  10.1088/1742-6596/848/1/012022

来源: IOP

【 摘 要 】

In this study we investigate the effect of triazavirine on ionic self-complementary (iSCM) containing peptides fibrils with transmission electron microscopy (TEM), small-angle neutron scattering (SANS) and MALDI mass-spectrometry (MS). It was shown that triazavirine is capable to dissociate iSCM amyloid fibrils. The mechanism of such an action is proposed.