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000015095 084__ $$2WoS$$aBiochemistry & Molecular Biology
000015095 1001_ $$0P:(DE-Juel1)VDB107233$$aHickman, D.T.$$b0$$uFZJ
000015095 245__ $$aSequence-independent control of peptide conformation in liposomal vaccines for targeting protein misfolding diseases
000015095 260__ $$aBethesda, Md.$$bSoc.$$c2011
000015095 300__ $$a13966 - 13976
000015095 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000015095 440_0 $$03091$$aJournal of Biological Chemistry$$v286$$x0021-9258
000015095 500__ $$aSolid-state NMR studies were supported by Netherlands Organization for Scientific Research Grant 700.26.121. D.R. is a member of the Board of Directors and Scientific Advisory Board of AC Immune SA.
000015095 520__ $$aSynthetic peptide immunogens that mimic the conformation of a target epitope of pathological relevance offer the possibility to precisely control the immune response specificity. Here, we performed conformational analyses using a panel of peptides in order to investigate the key parameters controlling their conformation upon integration into liposomal bilayers. These revealed that the peptide lipidation pattern, the lipid anchor chain length, and the liposome surface charge all significantly alter peptide conformation. Peptide aggregation could also be modulated post-liposome assembly by the addition of distinct small molecule β-sheet breakers. Immunization of both mice and monkeys with a model liposomal vaccine containing β-sheet aggregated lipopeptide (Palm1-15) induced polyclonal IgG antibodies that specifically recognized β-sheet multimers over monomer or non-pathological native protein. The rational design of liposome-bound peptide immunogens with defined conformation opens up the possibility to generate vaccines against a range of protein misfolding diseases, such as Alzheimer disease.
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000015095 650_2 $$2MeSH$$aAlzheimer Disease: metabolism
000015095 650_2 $$2MeSH$$aAnimals
000015095 650_2 $$2MeSH$$aCircular Dichroism
000015095 650_2 $$2MeSH$$aFemale
000015095 650_2 $$2MeSH$$aHumans
000015095 650_2 $$2MeSH$$aImmunoglobulin G: chemistry
000015095 650_2 $$2MeSH$$aLiposomes: chemistry
000015095 650_2 $$2MeSH$$aMagnetic Resonance Spectroscopy
000015095 650_2 $$2MeSH$$aMice
000015095 650_2 $$2MeSH$$aMice, Inbred C57BL
000015095 650_2 $$2MeSH$$aPeptides: chemistry
000015095 650_2 $$2MeSH$$aProtein Conformation
000015095 650_2 $$2MeSH$$aProtein Folding
000015095 650_2 $$2MeSH$$aProtein Structure, Secondary
000015095 650_2 $$2MeSH$$aProtein Structure, Tertiary
000015095 650_2 $$2MeSH$$aProteostasis Deficiencies: metabolism
000015095 650_2 $$2MeSH$$aThiazoles: chemistry
000015095 650_2 $$2MeSH$$aVaccines: chemistry
000015095 650_7 $$00$$2NLM Chemicals$$aImmunoglobulin G
000015095 650_7 $$00$$2NLM Chemicals$$aLiposomes
000015095 650_7 $$00$$2NLM Chemicals$$aPeptides
000015095 650_7 $$00$$2NLM Chemicals$$aThiazoles
000015095 650_7 $$00$$2NLM Chemicals$$aVaccines
000015095 650_7 $$02390-54-7$$2NLM Chemicals$$athioflavin T
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