Abstract:
: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, alpha-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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Efremov RG,Nolde DE,Volynsky PE,Chernyavsky AA,Dubovskii PV,Arseniev ASdoi
10.1016/s0014-5793(99)01505-7keywords:
subject
Has Abstractpub_date
1999-11-26 00:00:00pages
205-10issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01505-7journal_volume
462pub_type
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