Synthesis of fragment 7-20 of human gamma-interferon linked through a methionine residue to polyacrylic resin: use of the adduct as an immunogen.

A peptide corresponding to the amino acid sequence of human gamma-interferon, residues 7-20, was synthesized by a solid phase procedure using polyacrylic resin and methionine as anchor. Fluorenemethoxycarbonyl and t-butyloxycarbonyl strategies were compared. After completion of the synthesis, side chain deprotections were performed on the peptide still attached to the resin. The purity of the peptide linked to the matrix was determined by amino acid analysis and solid phase sequencing. The presence of methionine allowed the peptide to be detached from the support by CNBr cleavage. The immune responses of the free peptide, the peptide linked to bovine serum albumin and the peptide resin adduct were compared. Peptide bound to polyacrylamide gave similar results to those obtained using classical immunization procedures.