![SPATIAL STRUCTURE OF ANALOGUE [VAL5] OF OCTARPHIN MOLECULE](/upload/21232f297a57a5a743894a0e4a801fc3/journals/cover/f8c56688fa307e98584d30b341015d28.jpeg)
Baku, Azerbaijan
Baku, Azerbaijan
The spatial structure of analogue [Val5] 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 Thr1-Pro2-Leu3-Val4-Thr5-Leu6-Phe7-Lys8-NH2 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-Leu3-Val4-Val5-Leu6-Phe7-Lys8-NH2 was estimated on the low-energy conformations of this molecule. It is shown that the spatial structure of the octarphin molecule can be presented by 13 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
1. Nekrasova Yu.N., Sadovnikov V.B., Zolotarev Yu.A., Navolockaya E.V. Svoystva i mehanizm deystviya sinteticheskogo peptida oktarfina. Bioorganicheskaya himiya, 2010, t. 36, № 5, c. 638-645. [Nekhasova Yu.N., Sadovnikov V.B., Zolotarev Yu.A., Navolotskaya E.V. The properties and mechanism of action of the octarphin peptide. Journal of Bioorganic Chemistry, 2010, vol. 36, no. 5, pp. 638-645. (In Russ.)]
2. Novolockaya E.V. Mezhdunarodnaya konferenciya po bioorganicheskoy himii, biotehnologii i bionanotehnologii. M., 2014, 38 c. [Navolotskaya E.V. Octarphin - nonopioid peptid of the opioid orgin. International conference on bioorganic chemistry, biotechnology and bionanotechnology, 2014, 35 p. (In Russ.)]
3. IUPAC-IUB, Quantiby, Units and Symbols in Physical Chemistry. Blackwell Scientific Publications, 1988, vol. 39, no. 5.
4. Akhmedov N.A., Tagiyev Z.H., Hasanov E.M., Akverdieva G.A. Theoretical conformational analisis of the bovine adrenal medulla 12 residue peptide molecule. J. Molecular Structure, 2003, vol. 646, pp. 75-80.
5. Akhmedov N.A., Ismailova L.I., Agayeva L.N., Gocayev N.M. The spatial structure of the cardio active peptides. Peptid and Protein Research, 2010, vol. 11, pp. 87-93.
6. Gadzhieva Sh.N., Ahmedov N.A., Masimov E.A., Godzhaev N.M. Prostranstvennaya struktura molekuly Thr- Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2. Biofizika, 2013, t. 58, vyp. 4, c. 587-590. [Gadjieva Sh.N., Akhmedov N.A., Masimov E.A., Godjaev N.M. Spatial Structure of Thr-Pro-Ala-Glu-Asp-Phe-Met-Arg-Phe-NH2. Biophysics, 2013, vol. 58, pp. 587-590. (In Russ.)]
