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[Effect of a new antiviral compound 1-morpholinomethyltetrahydro-2(1H)-pyrimidinone on the interaction of influenza virus proteins with flat lipid membranes].

Abstract
The antiviral preparation 1-morpholinomethyltetrahydro-2(1H)-pyrimidinone (abbreviation DD-13) inhibiting reproduction of certain enveloped viruses belonging to groups of orthomyxoviruses and alphaviruses, influenza type A viruses among them, inhibited adsorption and insertion of influenza virus M protein into model bilayer lipid membranes. The preparation did not interact directly with lipid bilayers but, after pretreatment of M protein with it, inhibited M protein interaction with the membranes: adsorption and insertion into the bilayer DD-13 did not affect the interaction of influenza virus surface glycoproteins with the model lipid membranes. It is concluded that the DD-13 preparation, not interacting with the membranes directly, in native systems may modify the protein-lipid interactions at the stages of virus penetration into the cell, penetration of M protein-coated nucleocapsid into the cell nucleus through the nuclear membrane, as well as at the stage of virus particle assembly on the plasma membrane of the infected cell.
AuthorsV A Tverdislov, I G Kharitonenkov, S V Sukhanov, A S Galabov
JournalVoprosy virusologii (Vopr Virusol) 1988 May-Jun Vol. 33 Issue 3 Pg. 278-81 ISSN: 0507-4088 [Print] Russia (Federation)
Vernacular TitleO vliianii novogo protivovurusnogo soedineniia 1-morfolinometiltetragidro-2(1H)-pirimidinona na vzaimodeĭstvie belkov virusa grippa s ploskimi lipidnymi membranami.
PMID3176426 (Publication Type: Journal Article)
Chemical References
  • Antiviral Agents
  • Lipid Bilayers
  • M-protein, influenza virus
  • Pyrimidinones
  • Viral Matrix Proteins
  • 1-morpholinomethyl-tetrahydro-1(1H)-pyrimidinone
Topics
  • Adsorption
  • Antiviral Agents (pharmacology)
  • Drug Interactions
  • In Vitro Techniques
  • Influenza A virus
  • Lipid Bilayers (pharmacology)
  • Pyrimidinones (pharmacology)
  • Surface Properties
  • Viral Matrix Proteins (pharmacology)

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