Structural-Specificity Relationships of the Immunoglobulin Molecule and the Solid Phase Peptde Synthesis of Two Antigen-Binding Peptides
Tippett, Peter S.
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Recent immunoglobulin structural-functional information was reviewed with special emphasis on x-ray crystallographic data from the binding region of the antibody molecule. Structure-specificity relationships between phosphorylcholine binding immunoglobulins were discussed and possible immunoglobulin synthetic approaches including hypervariable region, active half-molecule, and half-molecule bi-layer syntheses were proposed. The course of the solid phase peptide syntheses of peptides including the first and third hypervariable regions of the heavy chain of M603 were followed by a modified form of the picrate monitoring procedure of Gisin and a Schwartz-Mann automated peptide synthesizer was modified to allow for complete automated cycling of this picrate monitoring procedure. "Normal" amino acid coupling characteric curves were defined and the coupling characteristics of a newly protected amino acid, Trp-For, were documented. Problems with the coupling of Asn and Arg were discussed and a mechanism for an unwanted side reaction involving the methionine side chain was studied. A method for estimating the number of deletion peptides contaminating the end product in solid phase peptide synthesis was proposed as was a new dimerization purification technique involving cysteine oxidation in peptides.