Hauptseite > Publikationsdatenbank > Sequence-independent control of peptide conformation in liposomal vaccines for targeting protein misfolding diseases > print

001     15095
005     20200402210018.0
024 7 _ |2 pmid
|a pmid:21343310
024 7 _ |2 pmc
|a pmc:PMC3077597
024 7 _ |2 DOI
|a 10.1074/jbc.M110.186338
024 7 _ |2 WOS
|a WOS:000289556200019
024 7 _ |a altmetric:1632216
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037 _ _ |a PreJuSER-15095
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |0 P:(DE-Juel1)VDB107233
|a Hickman, D.T.
|b 0
|u FZJ
245 _ _ |a Sequence-independent control of peptide conformation in liposomal vaccines for targeting protein misfolding diseases
260 _ _ |a Bethesda, Md.
|b Soc.
|c 2011
300 _ _ |a 13966 - 13976
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
|0 0
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336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
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336 7 _ |a article
|2 DRIVER
440 _ 0 |0 3091
|a Journal of Biological Chemistry
|v 286
|x 0021-9258
500 _ _ |a Solid-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.
520 _ _ |a Synthetic 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.
536 _ _ |0 G:(DE-Juel1)FUEK409
|2 G:(DE-HGF)
|a Funktion und Dysfunktion des Nervensystems
|c P33
|x 0
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|2 G:(DE-HGF)
|a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
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|x 1
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Alzheimer Disease: metabolism
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Circular Dichroism
650 _ 2 |2 MeSH
|a Female
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Immunoglobulin G: chemistry
650 _ 2 |2 MeSH
|a Liposomes: chemistry
650 _ 2 |2 MeSH
|a Magnetic Resonance Spectroscopy
650 _ 2 |2 MeSH
|a Mice
650 _ 2 |2 MeSH
|a Mice, Inbred C57BL
650 _ 2 |2 MeSH
|a Peptides: chemistry
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Protein Folding
650 _ 2 |2 MeSH
|a Protein Structure, Secondary
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 2 |2 MeSH
|a Proteostasis Deficiencies: metabolism
650 _ 2 |2 MeSH
|a Thiazoles: chemistry
650 _ 2 |2 MeSH
|a Vaccines: chemistry
650 _ 7 |0 0
|2 NLM Chemicals
|a Immunoglobulin G
650 _ 7 |0 0
|2 NLM Chemicals
|a Liposomes
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptides
650 _ 7 |0 0
|2 NLM Chemicals
|a Thiazoles
650 _ 7 |0 0
|2 NLM Chemicals
|a Vaccines
650 _ 7 |0 2390-54-7
|2 NLM Chemicals
|a thioflavin T
650 _ 7 |2 WoSType
|a J
700 1 _ |0 P:(DE-Juel1)VDB107234
|a López-Deber, M.P.
|b 1
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB107235
|a Ndao, D.M.
|b 2
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB107236
|a Silva, A.B.
|b 3
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB98426
|a Nand, D.
|b 4
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB72755
|a Pihlgren, M.
|b 5
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB72757
|a Giriens, V.
|b 6
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB107237
|a Madani, R.
|b 7
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB107238
|a St.-Pierre, A.
|b 8
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB98438
|a Karastan, H.
|b 9
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB72731
|a Nagel-Steger, L.
|b 10
|u FZJ
700 1 _ |0 P:(DE-Juel1)132029
|a Willbold, D.
|b 11
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB2263
|a Riesner, D.
|b 12
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB72768
|a Nicolau, C.
|b 13
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB77861
|a Baldus, M.
|b 14
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB72767
|a Pfeifer, A.
|b 15
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB72753
|a Muhs, A.
|b 16
|u FZJ
773 _ _ |0 PERI:(DE-600)1474604-9
|a 10.1074/jbc.M110.186338
|g Vol. 286, p. 13966 - 13976
|p 13966 - 13976
|q 286<13966 - 13976
|t The @journal of biological chemistry
|v 286
|x 0021-9258
|y 2011
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3077597
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