Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/6151
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dc.contributor.authorMerlino, A.en_us
dc.contributor.authorVitiello, G.en_us
dc.contributor.authorGrimaldi, M.en_us
dc.contributor.authorSica, F.en_us
dc.contributor.authorBusi, Elenaen_us
dc.contributor.authorBasosi, Riccardoen_us
dc.contributor.authorD’Ursi, A. M.en_us
dc.contributor.authorFragneto, G.en_us
dc.contributor.authorPaduano, L.en_us
dc.contributor.authorG. D’Errico, G.en_us
dc.date.accessioned2021-03-30T16:00:01Z-
dc.date.available2021-03-30T16:00:01Z-
dc.date.issued2012-
dc.identifier.issn1520-6106en_US
dc.identifier.urihttp://hdl.handle.net/20.500.12779/6151-
dc.description40769en_US
dc.description.abstractViral fusion glycoproteins present a membrane-proximal external region (MPER) which is usually rich in aromatic residues and exhibits a marked tendency to stably reside at the membrane interfaces, leading, through unknown mechanisms, to a destabilization of the bilayer structure. This step has been proposed to be fundamental for the fusion process between target membrane and viral envelope. In the present work, we investigate the interaction between an octapeptide (C8) deriving from the MPER domain of gp36 of feline immunodeficiency virus and POPC bilayers by combining experimental results obtained by neutron reflectivity, electron spin resonance, circular dichroism, and fluorescence spectroscopy with molecular dynamics simulations. Our data indicate that C8 binds to the lipid bilayer adsorbing onto the membrane surface without deep penetration. As a consequence of this interaction, the bilayer thickness decreases. The association of the peptide with the lipid membrane is driven by hydrogen bonds as well as hydrophobic interactions that the Trp side chains form with the lipid headgroups. Upon peptide-bilayer interaction, C8 forms transient secondary structures ranging from 3(10) helices to turn conformations, while acyl chains of the peptide-exposed POPC molecules assume a more ordered packing. At the same time, lipid headgroups' hydration increases. The asymmetric lipid bilayer perturbation is proposed to play a fundamental role in favoring the membrane fusion process.en_US
dc.language.isoenen_US
dc.relationNoneen_US
dc.relation.ispartofJOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICALen_US
dc.subjectDYNAMICS SIMULATIONS; TRANSMEMBRANE GLYCOPROTEIN,; PHOSPHOLIPID-BILAYERS; NEUTRON REFLECTIVITY; COMPUTER-SIMULATION; STRUCTURAL-ANALYSIS; MAGNETIC-RESONANCE; ROMATIC RESIDUES; PROXIMAL REGION; RIBONUCLEASE-Aen_US
dc.titleDestabilization of lipid membranes by a Peptide derived from Glycoprotein gp36 of feline immunodeficiency virus: a combined molecular dynamics/experimental studyen_US
dc.typeArticleen_US
dc.identifier.doi10.1021/jp204781aen_US
dc.identifier.scopus2-s2.0-84855835104en_US
dc.identifier.isiWOS:000298978100048en_US
dc.relation.volume116en_US
dc.relation.issue1en_US
dc.description.firstpage401en_US
dc.description.lastpage412en_US
dc.description.thirdmissionNot applicableen_US
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeArticle-
item.fulltextNo Fulltext-
crisitem.author.orcid0000-0003-1026-7668-
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