Influence of N-terminal amino acids and conjugation position to carrier on specificities of antibodies elicited by malaria peptides
Ramasamy, R.; Wickremaratne, C.
Indian Journal of Medical Research 99: 21-26
1994
ISSN/ISBN: 0019-5340 PMID: 8163297 Document Number: 432066
The specificity of murine antibodies raised against structurally related peptides derived from a malaria parasite membrane protein was studied. The peptides were conjugated to bovine serum albumin (BSA) with 6-maleimido caproic acyl N-hydroxysuccinimide ester before immunization. Conjugation to BSA through a C-terminal or an internal cysteine residue elicited antibodies with noticeably different specificities. An N-terminal tripeptide sequence arginine-asparagine-asparagine had a dominant influence on the immunogenicity of the peptides. Such factors need to be taken into consideration while designing peptide-based immunogens.