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Immunogenicity of dinitrocarboxyphenylated melittin: The influence of C‐terminal chain shortening, N‐terminal substitution and prolin insertion at positions 5 and 10
Author(s) -
Zhao Zhenjun,
Rolli Hanspeter,
Schneider Conrad H.
Publication year - 1995
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.310010206
Subject(s) - melittin , immunogen , immunogenicity , chemistry , conjugate , antibody , peptide , biochemistry , stereochemistry , biology , immunology , monoclonal antibody , mathematical analysis , mathematics
Peptides derived from the bee‐venom melittin were fitted with the haptenic group dinitrocarboxyphenyl(Dncp) and tested in out‐bred guinea pigs for immunogenicity by measuring the IgG anti‐Dncp antibody response by ELISA. Dncp‐conjugates comprising virtually the entire melittin proved to be strong immunogens producing antibody responses comparable to those of proteins. Weak responses were obtained with considerably shortened seqences. Conjugates with N‐terminal Dncp gave markedly reduced antibody responses compared to peptides with C‐terminal Dncp. An N‐terminal biotinyl substituent abolished the immune response whereas N‐terminal lauryl and caprylyl had little effect. Insertion of L‐proline into a hexadecapeptide conjugate abolishing the possibility of helix formation gave an immunogen to which individual animals clearly responded on a low level. Oligomerisation, but not the cytolytic activity of melittin peptides, may contribute to the immunogenicities observed.