The prolonged action of an insulin peptidomimetic by the substitution of L-amino acid for its D-isomer
Maslov, D.L.; Lokhov, P.G.; Abakumova, O.I.; Tsvetkova, T.A.; Prozorovskiĭ, V.N.
Voprosy Meditsinskoi Khimii 48(1): 103-110
2002
ISSN/ISBN: 0042-8809 PMID: 12068492 Document Number: 540729
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.