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dc.contributor.authorEskandari, Sharareh
dc.contributor.authorStephenson, Rachel J
dc.contributor.authorFuaad, Abdullah Ahmad
dc.contributor.authorApte, Simon H
dc.contributor.authorDoolan, Denise L
dc.contributor.authorToth, Istvan
dc.date.accessioned2017-08-11T05:20:19Z
dc.date.available2017-08-11T05:20:19Z
dc.date.issued2015
dc.identifier.issn0947-6539
dc.identifier.doi10.1002/chem.201404997
dc.identifier.urihttp://hdl.handle.net/10072/343860
dc.description.abstractDesigning a lipopeptide (LP) vaccine with a specific asymmetric arrangement of epitopes may result in an improved display of antigens, increasing host-cell recognition and immunogenicity. This study aimed to synthesise and characterise the physicochemical properties of a library of asymmetric LP-based vaccine candidates that contained multiple CD4+ and CD8+ T-cell epitopes from the model protein antigen, ovalbumin. These fully synthetic vaccine candidates were prepared by microwave-assisted solid phase peptide synthesis. The C12 or C16 lipoamino acids were coupled to the N or C terminus of the OVA CD4 peptide epitope. The OVA CD4 LPs and OVA CD8 peptide constructs were then conjugated using azide–alkyne Huisgen cycloaddition to give multivalent synthetic vaccines. Physiochemical characterisation of these vaccines showed a tendency to self-assemble in aqueous media. Changes in lipid length and position induced self-assembly with significant changes to their morphology and secondary structure as shown by transmission electron microscopy and circular dichroism.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherWiley
dc.relation.ispartofpagefrom1251
dc.relation.ispartofpageto1261
dc.relation.ispartofissue3
dc.relation.ispartofjournalChemistry - A European Journal
dc.relation.ispartofvolume21
dc.relation.urihttp://purl.org/au-research/grants/NHMRC/APP1037304
dc.relation.grantIDAPP1037304
dc.relation.fundersNHMRC
dc.subject.fieldofresearchChemical sciences
dc.subject.fieldofresearchMedicinal and biomolecular chemistry not elsewhere classified
dc.subject.fieldofresearchcode34
dc.subject.fieldofresearchcode340499
dc.titleSynthesis and characterisation of self-assembled and self-adjuvanting asymmetric multi-epitope lipopeptides of ovalbumin
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorEskandari, Sherry


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