Sequence-independent control of peptide conformation in liposomal vaccines for targeting protein misfolding diseases

Hickman, David T., Lopez-Deber, Maria Pilar, Mlaki Ndao, Dorin, Silva, Alberto B., Nand, Deepak, Pihlgren, Maria, Giriens, Valerie, Madani, Rime, St.-Pierre, Annie, Karastaneva, Hristina, Nagel-Steger, Luitgard, Willbold, Dieter, Riesner, Detlev, Nicolau, Claude, Baldus, Marc, Pfeifer, Andrea and Muhs, Andreas (2011) Sequence-independent control of peptide conformation in liposomal vaccines for targeting protein misfolding diseases. The Journal of Biological Chemistry, 286 16: 13966-13976. doi:10.1074/jbc.M110.186338

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Author Hickman, David T.
Lopez-Deber, Maria Pilar
Mlaki Ndao, Dorin
Silva, Alberto B.
Nand, Deepak
Pihlgren, Maria
Giriens, Valerie
Madani, Rime
St.-Pierre, Annie
Karastaneva, Hristina
Nagel-Steger, Luitgard
Willbold, Dieter
Riesner, Detlev
Nicolau, Claude
Baldus, Marc
Pfeifer, Andrea
Muhs, Andreas
Title Sequence-independent control of peptide conformation in liposomal vaccines for targeting protein misfolding diseases
Journal name The Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 2011-02-22
Sub-type Article (original research)
DOI 10.1074/jbc.M110.186338
Open Access Status File (Publisher version)
Volume 286
Issue 16
Start page 13966
End page 13976
Total pages 11
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2012
Language eng
Formatted abstract
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.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
Institute for Molecular Bioscience - Publications
 
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Citation counts: TR Web of Science Citation Count  Cited 21 times in Thomson Reuters Web of Science Article | Citations
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Created: Tue, 24 May 2011, 15:28:04 EST by Susan Allen on behalf of Institute for Molecular Bioscience