Synthesis and Characterization of New N-Terminal Bchain Modified Human Insulin Analogues

Abstract

New human insulin analogues were synthesized by fragment condensation reactions of N A1 , N B29 Msc protected native human insulin of different B-chain lengths with the dipeptide Boc-Asn-Thr-OH. Edman degradation was used to obtain shortened B-chain insulin intermediates. Purification of the products was achieved using gel filtration, ion exchange chromatography and RP-MPLC chromatography. Analysis of synthesized analogues accomplished by RP-HPLC chromatography and amino acid analysis. The modified insulin analogues with the amino acids Asparagine in the first position and Threonine in the second position of the N-terminal B-chain of insulin would be expected to show an enhanced T R* transition compared with that of wild-type structure.