Abstract
We demonstrate that a peptoid composed of five monomers and attached via a maleimide linker to a carrier protein elicits anti-peptoid, anti-linker and anti-carrier antibodies in rabbits. Specific anti-peptoid antibodies were affinity purified and used to reproducibly retrieve three specific peptoid-coupled beads from 20,000 irrelevant peptoid-beads using magnetic screening.
Highlights
Our long term goal is to generate vaccine candidates for any pathogen or toxin for which neutralizing polyclonal antibodies (PAbs) or monoclonal antibodies (MAbs) exist or could be made, without prior knowledge of the protective epitope(s)
ELISA plates were coated with R5 peptoid conjugated to an irrelevant carrier protein (R5-BSA, ); an irrelevant peptoid conjugated to BSA (RC-BSA, ∆) using the same linker as was used to link R5 to KLH used for immunization; BSA alone ( ); KLH alone (◊ with dotted line); and R5-KLH (♦)
We further confirmed the presence of anti-linker antibodies in the antiserum but not in the affinity purified rabbit anti-R5 (RAR5) by attaching an irrelevant carrier (BSA; Pierce) to the maleimide linker and testing the sera and affinity purified PAbs against ovalbumin or ovalbuminmaleimide by ELISA (Figure 4)
Summary
Our long term goal is to generate vaccine candidates for any pathogen or toxin for which neutralizing polyclonal antibodies (PAbs) or monoclonal antibodies (MAbs) exist or could be made, without prior knowledge of the protective epitope(s). Linker or carrier protein were present in the pre-immunization sera (data not shown). Antibodies against the intact peptoid, linker and carrier protein could be detected (Figure 3A).
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