Voprosy meditsinskoi khimii (ISSN 0042-8809)

The prolonged action of insulin analogue by the substitution of l-amino acids fortheir d-isomers

   


1. Orekhovich Institute of Biomedical Chemistry, Russian Academy of Medical Sciences
PubMed Id: 12068492
Year: 2002 vol: 48  issue:1  pages: 103-110
Abstract: The synthesized decapeptide represents functionally important site for binding to theinsulin receptor. Amino acid residues at position, 1-8 correlate with B-chain of insulinat position B19-B26, and the residues at position 9-10 correlate with A-chain at positionA20-A21. The new peptide was obtained by substitution of two aromatic L-amino acidresidues (B24 and B26) for their D-optical isomers. These peptides were tested with cellcultures L929 and PC12 (glucose uptake). Increased concentration of peptides correlatedwith stimulation of glucose uptake by cells. Studies carried out on animals withstreptosotocine-caused diabetes showed that, synthesized peptides were able to decreaseglucose level in blood, but decapeptide with D amino acid showed a more pronounced effectcompared to the decapeptide with L amino acid.
Download PDF:
Reference: Maslov D.L., Lokhov P.G., Abakumova O. YU., Tsvetkova T.A., Prozorovskiy V.N., The prolonged action of insulin analogue by the substitution of l-amino acids fortheir d-isomers, Voprosy meditsinskoi khimii, 2002, vol: 48(1), 103-110.
References
 2002(Vol:48)
 2001(Vol:47)
 2000(Vol:46)
 1999(Vol:45)
 1998(Vol:44)
 1997(Vol:43)
 1996(Vol:42)