Nonepitopic antibody binding sequence: implications in screening and development of peptide vaccines.
We describe the interaction of a nonepitopic synthetic decapeptide sequence comprising, GQVLQGAIKG, derived from a random sequence with polyclonal IgGs from various animal sources. GQVLQGAIKG was screened for antibody binding activity using ELISA techniques. The peptide showed similar binding characteristics to the IgGs tested. The results were similar whether we used peptide acid or amide. MAP (multiple antigen peptide)-type construct of the peptide was synthesised and employed as an approach to enhance peptide-IgG interaction. The construct, (GQVLQGAIKG)(4)-K(2)-K, showed significant antibody binding activity relative to its monomeric form. These results show that nonepitopic sequences may contribute to binding activity observed in peptide library screening and development of peptide based vaccines. As a cautionary point the measure of antibody binding cannot alone be used to classify peptide as an antigen.
Adesida
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Drug Delivery Group, School of Pharmacy & Pharmaceutical Sciences, University of Manchester, Oxford Road, Manchester, UK.
Aojula
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Aojula
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Clarke
D J
DJ
D000937:Antigen-Antibody Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes; D019151:Peptide Library; D011485:Protein Binding; D020539:Sequence Analysis, Protein; D014614:Vaccines, Synthetic
D000939:Epitopes; D019151:Peptide Library; D014614:Vaccines, Synthetic