SYNTHESIS AND CHARACTERIZATION OF NEW N-TERMINAL BCHAIN MODIFIED HUMAN INSULIN ANALOGUES | Zendy

Jewad K. Shneine | Zendy

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SYNTHESIS AND CHARACTERIZATION OF NEW N-TERMINAL BCHAIN MODIFIED HUMAN INSULIN ANALOGUES

Author(s) -

Jewad K. Shneine

Publication year - 2010

Publication title -

journal of al-nahrain university-science

Language(s) - English

Resource type - Journals

eISSN - 2519-0881

pISSN - 1814-5922

DOI - 10.22401/jnus.13.4.03

Subject(s) - edman degradation , size exclusion chromatography , chemistry , threonine , insulin , asparagine , amino acid , dipeptide , chromatography , high performance liquid chromatography , human insulin , aspartic acid , biochemistry , peptide sequence , stereochemistry , biology , serine , phosphorylation , endocrinology , gene , enzyme

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-AsnThr-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.

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