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Factors important for fusogenic activity of peptides: molecular modeling study of analogs of fusion peptide of influenza virus hemagglutinin
Author(s) -
Efremov Roman G.,
Nolde Dmitry E.,
Volynsky Pavel E.,
Chernyavsky Andrei A.,
Dubovskii Peter V.,
Arseniev Alexander S.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01505-7
Subject(s) - lipid bilayer fusion , hemagglutinin (influenza) , chemistry , peptide , biophysics , amphiphile , fusion , bilayer , membrane , lipid bilayer , biochemistry , biology , copolymer , organic chemistry , linguistics , philosophy , gene , polymer
Nine analogs of fusion peptide of influenza virus hemagglutinin whose membrane perturbation activity has been thoroughly tested [Murata et al. (1992) Biochemistry 31, 1986–1992; Murata et al. (1993) Biophys. J. 64, 724–734] were characterized by molecular modeling techniques with the aim of delineating any specific structural and/or hydrophobic properties inherent in peptides with fusogenic activity. It was shown that, regardless of characteristics common to all analogs (peripheral disposition at the water‐lipid interface, amphiphilic nature, α‐helical structure, etc.), only fusion active peptides reveal a specific ‘tilted oblique‐oriented’ pattern of hydrophobicity on their surfaces and a certain depth of penetration to the non‐polar membrane core. The conclusion was reached that these factors are among the most important for the specific destabilization of a bilayer, which is followed by membrane fusion.