[en] Various peptide segments have been modeled as asymmetric amphipathic
alpha-helices. Theoretical calculations have shown that they insert obliquely
into model membranes. They have been named "tilted peptides". Molecular modeling
results reported here also evidence the presence of tilted peptides in ADM-1
protein of Caenorhabditis elegans that may be involved in fusion events, in
meltrin alpha, a protein implicated in myoblast fusion, in hemagglutinin of
influenza virus, in the E2 glycoprotein of rubella virus, in the S protein of
hepatitis B virus, in a subdomain of Ebola virus and in the malaria CS protein.
Experimental results have indicated that tilted peptide fragments may be involved
in cellular life events like sperm-egg fecondation, muscle development, protein
translocation through signal sequences and cellular death caused by viral
infection or parasite infestation. We speculate that membrane destabilization by
these tilted peptides may be an important common step in life processes involving
fusion phenomena.
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