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Peptides bound to proteosomes via hydrophobic feet become highly immunogenic without adjuvants

Addition of either a lauroyl or a pentapeptide (FLLAV) hydrophobic foot to the NH2 terminus of a small, synthetic peptide allowed the peptide to hydrophobically complex to meningococcal outer membrane protein proteosomes by simple dialysis. Both conventional and LPS- hyporesponsive mice immunized wi...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1988
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188847/
https://www.ncbi.nlm.nih.gov/pubmed/3346624
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description Addition of either a lauroyl or a pentapeptide (FLLAV) hydrophobic foot to the NH2 terminus of a small, synthetic peptide allowed the peptide to hydrophobically complex to meningococcal outer membrane protein proteosomes by simple dialysis. Both conventional and LPS- hyporesponsive mice immunized with these complexes without any adjuvants developed high-titered and persistent anti-peptide IgG. Since proteosomes have been safely given to many people and since important antigenic determinants are generally hydrophilic, this system should be widely applicable to the development of peptide vaccines for human use.
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spelling pubmed-21888472008-04-17 Peptides bound to proteosomes via hydrophobic feet become highly immunogenic without adjuvants J Exp Med Articles Addition of either a lauroyl or a pentapeptide (FLLAV) hydrophobic foot to the NH2 terminus of a small, synthetic peptide allowed the peptide to hydrophobically complex to meningococcal outer membrane protein proteosomes by simple dialysis. Both conventional and LPS- hyporesponsive mice immunized with these complexes without any adjuvants developed high-titered and persistent anti-peptide IgG. Since proteosomes have been safely given to many people and since important antigenic determinants are generally hydrophilic, this system should be widely applicable to the development of peptide vaccines for human use. The Rockefeller University Press 1988-02-01 /pmc/articles/PMC2188847/ /pubmed/3346624 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Peptides bound to proteosomes via hydrophobic feet become highly immunogenic without adjuvants
title Peptides bound to proteosomes via hydrophobic feet become highly immunogenic without adjuvants
title_full Peptides bound to proteosomes via hydrophobic feet become highly immunogenic without adjuvants
title_fullStr Peptides bound to proteosomes via hydrophobic feet become highly immunogenic without adjuvants
title_full_unstemmed Peptides bound to proteosomes via hydrophobic feet become highly immunogenic without adjuvants
title_short Peptides bound to proteosomes via hydrophobic feet become highly immunogenic without adjuvants
title_sort peptides bound to proteosomes via hydrophobic feet become highly immunogenic without adjuvants
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188847/
https://www.ncbi.nlm.nih.gov/pubmed/3346624