Le. Panin et al., DESIGN, SYNTHESIS, AND IMMUNOCHEMICAL IDENTIFICATION OF THE PUTATIVE RECEPTOR DOMAIN OF HUMAN INSULIN, Molecular biology, 31(2), 1997, pp. 309-313
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.