PMID: 8589546Sep 1, 1995Paper

Elucidation of monoclonal antibody polyspecificity using a synthetic combinatorial library

Peptide Research
C PinillaR Houghten

Abstract

The potential polyspecificity of an antipeptide monoclonal antibody was systematically examined using a soluble synthetic combinatorial library (SCL). This SCL was composed of 400 different hexapeptide mixtures, each of which consisted of more than 130,000 peptides totalling 50 million individual sequences in approximately equimolar concentration. The 400 peptide mixtures making up this SCL were screened by competitive enzyme-linked immunosorbent assay (ELISA) for their ability to inhibit monoclonal antibody binding to the original immunizing peptide. Individual peptides were derived from three different peptide mixtures of the peptide library through an iterative screening and selection process. In addition to the identification of the six-residue antigenic determinant recognized by this monoclonal antibody, two other hexapeptides were found to have binding affinities 5- to 10-fold higher than the original antigenic determinant sequence. These peptide sequences represent analogs in which a polar amino acid (threonine) in the original antigenic determinant was substituted with a large, aromatic amino acid (either tryptophan or tyrosine). Peptide analogs of the antigenic determinant, ranging from single to multiple substitutions...Continue Reading

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