Published May 2017 | Version v1
Journal article Metadata-only

Structural features of the ionic self-complementary amyloidogenic peptide

Creators

  • 1. DMRB PNPI NRC KI, Gatchina (Russian Federation)
  • 2. Influenza Institute MH of Russia, Saint-Petersburg (Russian Federation)
  • 3. Joint Institute for Nuclear Research, Dubna (Russian Federation)

Description

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. (paper)

Availability note (English)

Available from http://dx.doi.org/10.1088/1742-6596/848/1/012022

Additional details

Identifiers

DOI
10.1088/1742-6596/848/1/012022;

Publishing Information

Journal Title
Journal of Physics. Conference Series (Online)
Journal Volume
848
Journal Issue
1
Journal Page Range
[7 p.]
ISSN
1742-6596

Conference

Title
3. international conference on small angle neutron scattering dedicated to the 80 anniversary of Yu.M. Ostanevich
Dates
6-9 Jun 2016
Place
Dubna (Russian Federation)

INIS

Country of Publication
United Kingdom
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
49012341
Subject category
S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
Resource subtype / Literary indicator
Conference
Descriptors DEI
ELECTRONS; MASS SPECTROSCOPY; NEUTRON DIFFRACTION; NEUTRONS; PEPTIDES; SMALL ANGLE SCATTERING; TRANSMISSION ELECTRON MICROSCOPY
Descriptors DEC
BARYONS; COHERENT SCATTERING; DIFFRACTION; ELECTRON MICROSCOPY; ELEMENTARY PARTICLES; FERMIONS; HADRONS; LEPTONS; MICROSCOPY; NUCLEONS; ORGANIC COMPOUNDS; PROTEINS; SCATTERING; SPECTROSCOPY