General Method for the Rapid Solid-Phase Synthesis of Large Numbers of Peptides: Specificity of Antigen--Antibody Interaction at the Level of Individual Amino Acids

• Published in: Proceedings of the National Academy of Sciences - PNAS 1985-08, Vol.82 (15), p.5131-5135
• Main Author: Houghten, Richard A.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Amino acids; Antibodies; Antibodies, Monoclonal - immunology; Antibody Specificity; Antigen-antibody reactions, antigen-antibody complexes, antibody-complement and others. Study of affinity. Antigen presentation; Antigens; Antigens, Viral - immunology; Biological and medical sciences; Enzyme linked immunosorbent assay; Epitopes; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Hydrophobicity; Immunology; Molecular immunology; Molecules; Monoclonal antibodies; Oligopeptides - chemical synthesis; Oligopeptides - immunology; Orthomyxoviridae - immunology; Resins; Structure-Activity Relationship; Washing
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.82.15.5131

A novel yet simple method is described that facilitates the synthesis of large numbers of peptides to the extent that the synthesis process need no longer be the limiting factor in many studies involving peptides. By using the methods described, 10-20 mg of 248 different 13-residue peptides representing single amino acid variants of a segment of the hemagglutinin protein (HA1) have been prepared and characterized in less than 4 weeks. Through examination of the binding of these analogs to monoclonal antibodies raised against residues 75-110 of HA1, it was found that a single amino acid, aspartic acid at position 101, is of unique importance to the interaction. Two other residues, aspartic acid-104 and alanine-106, were found to play a lesser but significant role in the binding interaction. Other single positional residue variations appear to be of little or no importance.