Peptide side chains topology plays a central role in peptide antigenicity, and antibody recognition is preserved with peptide mimics resembling the parent peptide original side chains stereochemical arrangement. Recent work from our group suggested that peptide antigens could be sequence-simplified while maintaining at least part of the antigenic properties of the parent peptide. Synthetic variants of antigenic peptides, one lacking of the side chains in the sequence odd position and the other in even position, prepared by replacing amino acid residues in the parent peptide with glycine residues alternatively in the sequence, cross-reacted to a significant extent with antibodies raised against the parent peptide. In addition, polyclonal antibodies raised in rabbits against the two sequence simplified were able to recognize with similar affinity and specificity the parent peptide, as well as other chimeric peptides containing the alternate pattern of amino acids. Results cumulatively suggest the possibility of redesigning peptide antigens in two variants which could preserve antigenicity as well as immunogenicity to a similar extent as the parent peptide.
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