Baku, Azerbaijan
By the method of the theoretic conformational analysis the conformational capabilities of the cytochrophin-4 molecule (Tyr1-Pro2-Phe3-Thr4) 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 cytochrophin-4 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 cytochrophin-4 molecule can be represented by the conformations of four shapes of the peptide backbone. The results obtained can be used to elucidate the structural and structural-functional organization of cytochrophin-4 molecules.
exorphin, cytochrophin-4, 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, № 1, s. 22-46. @@Chesnokova E.A., Sarycheva N.Y., DubyninV.A., KamenskyA.A. Food-Derived Opioid Peptides and Their Neurological Impact. Advancesin Physiological Sciences, 2015, vol. 46, no. 1, pp. 22-46. (In Russ.)
2. Sokolov O.Yu., Kost N. V., Andreeva O.O., Korneeva E.V., Meshavkin V.K., Tarakanova Yu.N., Zolotarev Yu.A., Grachev S.A., Miheeva I.G., Zozulya A.A. Vozmozhnaya rol' kazomorfinov v patogeneze autizma. Psihiatriya, 2010, t. 45, № 3, s. 29-35. @@Sokolov O.Yu., Kost N.V., Andreeva O.O., Korneeva E.V., MeshavkinV.K., Tarakanova Yu.N., Zolotarev Yu.A., Grachev S.A., Mikheeva I.G., Zozulya A.A. The possibl eroleof casomorphin sinpathogenesis of autism. Psixiatriya, 2010, vol. 46, no. 3, pp. 29-35. (In Russ.)
3. Lew R.A., Mustafa T., Ye S. et al. Angiotensin AT4 ligands are potent, competitive inhibitors of insulin regulated aminopeptidase (IRAP). J. of Neurochemistry, 2003, vol. 86, no. 2, pp. 344-350.
4. 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.)
5. 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. Bioorganic chemistry, 1990, vol. 16, pp. 649-667. (In Russ.)
6. Akhmedov N.A., Agayeva L.N., Ismailova L.I., Godjaev N.M. Thespatial structure of the cardio active peptides. Current Topics in Peptide and Protein Research, 2010, vol. 11, pp. 87-93.
7. 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.)
8. 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.
9. Hasanov E.M., Akhmedov N.A. Spatial Structure of Peptide BAM-20P.International Journal of Innovative Science and Research Technology, 2018, iss. no. 4-2456-2165, vol. 3, pp. 72-76.
10. 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, pp. 201-104.
11. IUPAC-IUB. Quantities, Units and Symbols in Physical Chemistry, Blackwell Scientific, Oxford 1993.
