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Title: Characterization of oligomerization of a peptide from the ebola virus glycoprotein by small-angle neutron scattering

Transmission electron microscopy (TEM) and small-angle neutron scattering (SANS) studies showed that model peptides QNALVCGLRQ (G33) and QNALVCGLRG (G31) corresponding to region 551–560 of the GP protein of the Sudan Ebola virus are prone to oligomerization in solution. Both peptides can form amyloid-like fibrills. The G33 peptide forms fibrils within one day of incubation, whereas the fibrillogenesis of the G31 peptide is observed only after incubation for several months. The possible role of the observed processes in the pathogenesis and the possibility of applying a combination of the TEM and SANS techniques to search for new compounds that are able to influence the protein oligomerization are discussed.
Authors:
 [1] ;  [2] ;  [3] ;  [2] ; ;  [1] ;  [2]
  1. National Research Center “Kurchatov Institute”, Konstantinov Petersburg Nuclear Physics Institute (Russian Federation)
  2. Ministry of Health of the Russian Federation, Research Institute of Influenza (Russian Federation)
  3. Joint Institute for Nuclear Research (Russian Federation)
Publication Date:
OSTI Identifier:
22471918
Resource Type:
Journal Article
Resource Relation:
Journal Name: Crystallography Reports; Journal Volume: 61; Journal Issue: 1; Other Information: Copyright (c) 2016 Pleiades Publishing, Inc.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; 60 APPLIED LIFE SCIENCES; GLYCOPROTEINS; INCUBATION; NEUTRON DIFFRACTION; PATHOGENESIS; PEPTIDES; SMALL ANGLE SCATTERING; SUDAN; TRANSMISSION ELECTRON MICROSCOPY; VIRUSES