% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Hickman:15095,
      author       = {Hickman, D.T. and López-Deber, M.P. and Ndao, D.M. and
                      Silva, A.B. and Nand, D. and Pihlgren, M. and Giriens, V.
                      and Madani, R. and St.-Pierre, A. and Karastan, H. and
                      Nagel-Steger, L. and Willbold, D. and Riesner, D. and
                      Nicolau, C. and Baldus, M. and Pfeifer, A. and Muhs, A.},
      title        = {{S}equence-independent control of peptide conformation in
                      liposomal vaccines for targeting protein misfolding
                      diseases},
      journal      = {The journal of biological chemistry},
      volume       = {286},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-15095},
      pages        = {13966 - 13976},
      year         = {2011},
      note         = {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.},
      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.},
      keywords     = {Alzheimer Disease: metabolism / Animals / Circular
                      Dichroism / Female / Humans / Immunoglobulin G: chemistry /
                      Liposomes: chemistry / Magnetic Resonance Spectroscopy /
                      Mice / Mice, Inbred C57BL / Peptides: chemistry / Protein
                      Conformation / Protein Folding / Protein Structure,
                      Secondary / Protein Structure, Tertiary / Proteostasis
                      Deficiencies: metabolism / Thiazoles: chemistry / Vaccines:
                      chemistry / Immunoglobulin G (NLM Chemicals) / Liposomes
                      (NLM Chemicals) / Peptides (NLM Chemicals) / Thiazoles (NLM
                      Chemicals) / Vaccines (NLM Chemicals) / thioflavin T (NLM
                      Chemicals) / J (WoSType)},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21343310},
      pmc          = {pmc:PMC3077597},
      UT           = {WOS:000289556200019},
      doi          = {10.1074/jbc.M110.186338},
      url          = {https://juser.fz-juelich.de/record/15095},
}