![Spatial organization of the analogue [PRO3] of octarphin molecule](/upload/21232f297a57a5a743894a0e4a801fc3/journals/cover/f8c56688fa307e98584d30b341015d28.jpeg)
The spatial structure of analogue [Pro3] of octarphin molecule has been investigated using theoretical conformational analysis method. Amino acid sequence Thr1-Pro2-Leu3-Val4-Thr5-Leu6-Phe7-Lys8-NH2 of octarphin conforms to the fragment 12-19 of β-endorphin. It is established that octarphin is related to macrophages of high affinity and specificity. Spatial structure of octarphin molecule has been investigated by method of theoretical conformational analysis. Calculations of conformational states of octarphin molecule are carried out regarding nonvalent, electrostatic and torsional interactions, hydrogen bonds as well. The spatial structure of the molecule Thr1-Pro2-Pro3-Val4-Thr5-Leu6-Phe7-Lys8-NH2 was estimated on the low-energy conformations of octarphin molecule. It is shown that the spatial structure of analogue [Pro3] of octarphin molecule can be presented by 3 low-energy forms of the main chain. The low-energy conformations of this molecule, the values of dihedral angles of the backbone and side chains of the amino acid residues were founded and the energies of intra- and inter-residual interactions were determined.
octarphin, analogue, theoretical conformational analysis, spatial structure, conformation
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