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  • Title: [Synthesis of insulin fragments and study of their physicochemical and immunological properties].
    Author: Panin LE, Tuzikov FV, Poteriaeva ON, Maksiutov AZ, Tuzikova NA, Sabirov AN.
    Journal: Bioorg Khim; 1997 Dec; 23(12):953-60. PubMed ID: 9499371.
    Abstract:
    A two-chain peptide was predicted as a receptor binding site of insulin on the basis of theoretical conformational analysis. This dimeric peptide, consisting of the C-terminal A18-A21 tetrapeptide of the insulin A-chain and the C-terminal B17-B30 tetradecapeptide of the insulin B-chain connected with a disulfide bridge, was synthesized along with the C-terminal nonadecapeptide. The analysis of the aggregation state of human insulin and the synthesized linear and dimeric peptides was performed by the small-angle X-ray scattering method. Specific antibodies were produced after rabbit immunization with the dimeric peptide-BSA conjugate. The immunochemical identity of the model dimeric peptide and the corresponding fragment of the insulin molecule were shown by immunoenzyme analysis.
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