DESIGN, SYNTHESIS, AND IMMUNOCHEMICAL IDENTIFICATION OF THE PUTATIVE RECEPTOR DOMAIN OF HUMAN INSULIN

A bipartite peptide supposedly representing the receptor-binding domai n of human insulin was chosen on the basis of theoretical analysis of the structural-functional organization of the insulin molecule, and sy nthesized chemically. The resulting construct comprised the C-terminal tetrapeptide of the A chain (A18-A21: NYCN) and the C-terminal tetrad ecapeptide of the B chain (B17-B30: LVCGERGFFYTPKT) connected by a dis ulfide bond. Upon administration to laboratory animals together with i nsulin, it exhibited a pronounced contrainsulin effect. Rabbit immuniz ation with the peptide (conjugated with bovine serum albumin) induced specific antibodies. Immunoenzyme analysis testified to the immunochem ical identity of the model peptide and the corresponding part of the i nsulin molecule.