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dc.contributor.authorZaman, Mehfuzen_US
dc.contributor.authorM. Abdel-Aal, Abu-Bakeren_US
dc.contributor.authorS.M. Phillipps, Karenen_US
dc.contributor.authorFujita, Yoshioen_US
dc.contributor.authorGood, M.en_US
dc.contributor.authorToth, Istvanen_US
dc.date.accessioned2017-05-03T15:04:58Z
dc.date.available2017-05-03T15:04:58Z
dc.date.issued2010en_US
dc.date.modified2011-04-07T05:32:31Z
dc.identifier.issn0264410Xen_US
dc.identifier.doi10.1016/j.vaccine.2009.12.046en_AU
dc.identifier.urihttp://hdl.handle.net/10072/38011
dc.description.abstractIncorporation of lipoamino acids (LAAs) into peptide structures effectively imparts self-adjuvanting activity onto otherwise ineffective immunogens. Our fully synthetic lipopeptide vaccine candidates against group A streptococcus (GAS) were composed of J14 as a target GAS B-cell epitope alongside a universal helper T-cell epitope (P25) and a LAA-based lipid moiety. In the current study, we investigated the ability of our lipopeptides to activate nuclear factor-kappaB (NF-kappaB) in a toll-like receptor-2 (TLR2)-dependent manner as the possible mode of action and reported the structure-function requirements for novel TLR2 targeting lipopeptides based on LAAs. The NF-kappaB activation was dependent on the dose and the length of the alkyl chains of the incorporated lipid moieties with the hierarchy LAA 3 (16 carbons)>LAA 2 (14 carbons)>LAA 1 (12 carbons). The position of the lipid moiety (C-terminus vs. N(epsilon)-terminus of the central lysine residue) does not significantly affect NF-kappaB activation. Lipopeptides containing different copies of LAA 3 were synthesized and the di-lipidated analogue was the most effective in NFkappaB activation.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherElsevieren_US
dc.publisher.placeUnited Kingdomen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom2243en_US
dc.relation.ispartofpageto2248en_US
dc.relation.ispartofissue10en_US
dc.relation.ispartofjournalVaccineen_US
dc.relation.ispartofvolume28en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchInfectious Diseasesen_US
dc.subject.fieldofresearchcode110309en_US
dc.titleStructure-activity relationship of lipopeptide Group A streptococcus (GAS) vaccine candidates on toll-like receptor 2en_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2010
gro.hasfulltextNo Full Text


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