A conformational analysis of biologically active RGD-containing cyclopentapeptides |
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Authors: | P V Kostetsky I V Artem’ev |
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Institution: | (1) Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117871 GSP-7 Moscow, Russia |
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Abstract: | The theoretical conformational analysis of the biologically active RGD-containing pentapeptide cyclo(-Arg-Gly-Asp-Phe-DVal-), an inhibitor of laminin P1 interaction with its receptor, was performed. The space of permissible torsional angles
of the backbone of the molecule was studied by the Monte Carlo method. From the large number of predicted low-energy conformers
with various packings of the cyclic moiety of this pentapeptide, only those were selected that corresponded to stable structures
of the model linear tripeptide Ac-Ala-Gly-Asp-NHMe. This peptide simulated the spatial possibilities of the backbones of RGD-containing
fragments of laminin, vitronectin, and fibronectin. We selected several dozen structures that may be potential biologically
active conformers, but only a few of them were capable of forming stable intramolecular hydrogen bonds. We assumed that a
biologically active conformer of cyclo(-Arg-Gly-Asp-Phe-DVal-) can be present in significant amounts in an equilibrium mixture in solution along with other conformers without necessarily
dominating among them. |
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Keywords: | cyclopeptides theoretical conformational analysis RGD-peptides |
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