By the method of the theoretic conformational analysis the conformational capabilities of the soymorphin-7 (Tyr1-Pro2-Tyr3-Val4-Val5-Asn6-Ala7-NH2) molecule were studied. The potential function of the system is chosen as the sum of non-valent, electrostatic and torsion interactions and the energy of hydrogen bonds. Low-energy conformations of the soymorphin-7 molecule, the values of the dihedral angles of the main and side chains of amino acid residues that make up the molecules are founded; the energy of intra- and inter-residual interactions is estimated. It is shown that the spatial structure of the soymorphin-7 molecule can be represented by eight conformations.
exorphin, soymorphin, opioid, structure, conformation
1. Chesnokova E.A., Sarycheva N.Yu., Dubynin V.A., Kamenskiy A.A. Opioidnye peptidy, poluchaemye s pischey i ih vliyanie na nervnuyu sistemu. Uspehi fiziologicheskih nauk, 2015, t. 46, nomer 1, s. 22-46. @@[Chesnokova E.A., Sarycheva N.Y., Dubynin V.A., Kamensky A.A. Food-Derived Opioid Peptidesand Their Neurological Impact. Advances in Physiological Sciences, 2015, vol. 46, no. 1, pp. 22-46. (In Russ.)]
2. De Azevedo E. Risks and controversies in the social construction of the concept of healthy food: the case of soy. Rev Saude Publica, 2011, vol. 45, no. 4, pp. 1-7.
3. Kaneko K., Iwaski M., Yoshikawa M., Ohinata K. Orally administered soymorphins, soy-derived opioid peptides. Am. J. Physiol. Gastrointest. Liver Physiol, 2010, vol. 299, no. 3, pp. G799-G805.
4. Ohinata K., Agui S., Yoshikawa M. Soymorphins, novel mu opioidpeptides derived from soy beta-conglycinin beta-subunit, have anxiolytic activities. Biosci. Biotechnol. Biochem, 2007, vol. 71, no. 10, pp. 2618-2621.
5. Yang S., Sonoda S., Chen L., Yoshikawa M. Structure-activity relationship of rubiscolins as delta opioid peptides. Peptides, 2003, vol. 24, no. 4, pp. 503-508.
6. Yang S., Yunden J., Sonoda S. et al. Rubiscolin, a delta selective opioid peptide derived from plant Rubisko. FEBSLett, 2001, vol. 509, pp. 213-217.
7. Ahmedov N.A. Teoreticheskiy konformacionnyy analiz molekul β-kazomorfina, valmuceptina i morficeptina. Molekulyarnaya Biologiya, 1989, t. 23, s. 240-248. @@[Akhmedov N.A. Teoretical conformation analysis of β-cazomorphin, valmuceptin and morphiceptin molecules. Molecular. Biol., 1989, vol. 23, pp. 240-240. (In Russ.)].
8. Ahmedov N.A., Godzhaev N.M., Suleymanova E.V., Popov E.M. Strukturnaya organizaciya molekul [Met] enkefalina i endorfinov. Bioorganicheskaya himiya, 1990, t. 16, s.649-667. @@[Akhmedov N.A., Godjaev N.M., Suleymanova E.V., Popov E.M. Structural organization of the [Met] encephalin and endorphins molecules. Bioorganicheskaya himiya, 1990, vol. 16, pp. 649-667. (In Russ.)].
9. Akhmedov N.A., Agayeva L.N., Ismailova L.I., Godjaev N.M. The spatial structure of the cardio active peptides. Current Topics in Peptide and Protein Research, 2010, vol. 11, pp. 87-93.
10. 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, s. 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.)].
11. Akhmedov N.A., Ismailova L.I., Abbasli R.M. et al. Spatial Structure of Octarphin molecule. IOSR J. Applied Physics (IOSR-JAP), 2016, vol. 8, pp. 66-70.
12. Hasanov E.M., Akhmedov N.A. Spatial Structure of Peptide BAM-20P. International Journal of Innovative Science and Research Technology, 2018, vol. 3, pp. 72-76.
13. Akhmedov N.A., Abbasli R.M., Agayeva L.N., Ismailova L.I. Three-dimensional structure of exorpin B5 molecule. Conference proceedings Modern Trends in Physics, 2019, 201 p.
14. IUPAC-IUB, Quantity, Units and Symbols in Physical Chemistry. Blackwell Scientific Publications, Oxford, 1988, vol. 39.
