[New water-soluble analog of the fusion peptide of influenza virus hemagglutinin: synthesis and properties].
A water-soluble analogue F32 of the fusion peptide from the influenza virus hemagglutinin was synthesized. It consisted of 32 aa residues and retained the ability to interact with lipid membranes; its N-terminal sequence 1-24 coincided with that of the fusion protein from hemagglutinin (strain A/PR/8/34), whereas residues 25-32 (GGGKKKKK) provided its solubility in water. The peptide induced the conductivity fluctuations in planar bilayer lipid membranes characteristic of active fusion peptides. Conditions were found using CD spectroscopy under which the structure of F32 inside detergent micelles, where it can be studied by high-resolution 1H NMR spectroscopy, is close to the structure of the peptide during its interaction with phospholipid liposomes. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2004, vol. 30, no. 2; see also http://www.maik.ru.
Dubovskiĭ
P V
PV
Shemyakin-Ovchinnikov, Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997 Russia. peter@nmr.ru
Zhmak
M N
MN
Maksaev
G I
GI
Arsen'ev
A S
AS
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D012995:Solubility; D014867:Water
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D010455:Peptides; D014867:Water