VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

The prolonged action of insulin analogue by the substitution of L-amino acids fortheir D-isomers

   
Maslov D.L.1, Lokhov P.G.1, Abakumova O. YU.1, Tsvetkova T.A.1, Prozorovskiy V.N.1

1. Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences
PubMed Id: 12068492
Year: 2002  Volume: 48  Issue: 1  Pages: 103-110
The synthesized decapeptide represents functionally important site for binding to the insulin receptor. Amino acid residues at position, 1-8 correlate with B-chain of insulin at position B19-B26, and the residues at position 9-10 correlate with A-chain at position A20-A21. The new peptide was obtained by substitution of two aromatic L-amino acid residues (B24 and B26) for their D-optical isomers. These peptides were tested with cell cultures L929 and PC12 (glucose uptake). Increased concentration of peptides correlated with stimulation of glucose uptake by cells. Studies carried out on animals with streptosotocine-caused diabetes showed that, synthesized peptides were able to decrease glucose level in blood, but decapeptide with D amino acid showed a more pronounced effect compared to the decapeptide with L amino acid.
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Maslov, D. L., Lokhov, P. G., Abakumova, O. , YU., Tsvetkova, T. A., Prozorovskiy, V. N. (2002). The prolonged action of insulin analogue by the substitution of L-amino acids fortheir D-isomers. Voprosy Meditsinskoi Khimii, 48(1), 103-110.
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