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Improved Detection of Human Antibodies to a Plasmodium Antigen Using a Peptide Modified with Aib Residues
Author(s) -
Bossus Marc,
Mohammed Lbachir,
Londono Arthuro,
Barbier Bernard,
Tartar André,
Druilhe Pierre,
GrasMasse Héléne
Publication year - 1997
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/(sici)1099-1387(199701)3:1<47::aid-psc80>3.0.co;2-v
Subject(s) - antigenicity , peptide , chemistry , residue (chemistry) , antibody , peptide sequence , antigen , biochemistry , stereochemistry , amino acid , microbiology and biotechnology , biology , immunology , gene
A 17‐mer sequence was selected as a model to study the influence of modifications of terminal ends both on the conformation of a peptide and on its antigenicity towards naturally developing antibodies. This sequence corresponded to a tandemly repeated motif, found in a long repetitive region, with high helical propensity, of a Plasmodium falciparum liver‐stage antigen (LSA‐1), immunogenic in man. Our model peptide was synthesized with ionizable or non‐ionizable ends, or modified in both extremities by introduction of the helix‐promoting residue α‐aminoisobutyric acid (Aib). Helical contribution, absent in the 17 amino‐acid sequence possessing ionizable ends, was detectable when non‐ionizable ends were introduced, and dramatically increased in the Aib‐modified analogue. The presence of ionizable ends totally abolished reactivity towards human sera, otherwise detectable with the peptide possessing non‐ionizable ends. While modification by Aib residues was neither detrimental nor beneficial to antigenicity in solution, it clearly resulted in an improved sensitivity of the specific antibody detection when used as solid‐phase antigen in ELISA. © 1997 European Peptide Society and John Wiley & Sons, Ltd.