The Spatial Structure of the ACTH-(7–10) Molecule

Agayeva, L.; Abdinova, A.; Akhmedova, S.; Akhmedov, N.

doi:10.1134/s0006350921040023

“…Нами были исследованы структурно-функциональные организации опиоидных пептидов энкефалинов, эндорфинов, эндоморфинов, динорфинов, неоэндорфинов, адренорфина, а в настоящее время исследуется пространственная структура экзорфинов. Эта работа является продолжением наших предыдущих исследований [4][5][6][7][8][9][10][11][12].…”

Section: структурная организация молекул сойморфиновunclassified

Structural Organization of Soymorphin Molecules

Akhmedov,

Agayeva,

Ismailova

2024

Russian Journal of Biological Physics and Chemisrty

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The conformational capabilities of soymorphine-5 (Thr1-Pro2-Phe3-Val4-Val5-NH2), soymorphine-6 (Tyr1-Pro2-Phe3-Val4-Val5-Asn6-NH2) and soymorphine-7 (Tyr1- Pro2-Tyr3-Val4-Val5-Asn6-Ala7-NH2) molecules have been studied by the method of theoretical conformational analysis. The potential function of the system is chosen as the sum of non-valence, electrostatic and torsion interactions and the energy of hydrogen bonds. The low-energy conformations of soymorphine-5, soymorphine-6 and soymorphine-7 molecules were found, the dihedral angles of the main and side chains of amino acid residues that make up the molecule were found, and the energy of intra- and interresidual interactions was estimated. Thus, the spatial structure of soymorphine-5, soymorphine-6 and soymorphine-7 molecules can be represented by eight structural types. It can be assumed that the molecules perform their physiological functions in these structures. Comparison of the low-energy structures of soymorphins shows that in all molecules the first four low-energy conformations are representatives of the structural types efef, efee, efff, effe for soymorphine-5, effff, efeff, efffe, effee for soymorphine-6, efffff, efeffe, efffef, effeee for soymorphine-6. soymorphine-7. On the basis of these structures, it is possible to propose their artificial analogues for synthesis. It was shown that the spatial structure of soymorphine-5, soymorphine-6 and soymorphine-7 molecules is represented by the conformations of eight shapes of the peptide skeleton. The results obtained can be used to elucidate the structural and structural-functional organization of soymorphine molecules.

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“…Нами были исследованы структурно-функциональные организации опиоидных пептидов энкефалинов, эндорфинов, эндоморфинов, динорфинов, неоэндорфинов, адренорфина, а в настоящее время исследуется пространственная структура экзорфинов. Эта работа является продолжением наших предыдущих исследований [4][5][6][7][8][9][10][11][12].…”

unclassified

Structural Organization of Lactoferroxin Molecules

Agayeva,

Abdinova,

Akhmedova

et al. 2024

Russian Journal of Biological Physics and Chemisrty

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The conformational possibilities of lactoferroxin A (H-Tyr1-Leu2-Gly3-Ser4-Gly5-Tyr6-OH) and lactoferroxin B (H-Arg1-Tyr2-Tyr3-Gly4-Tyr5-OH) molecules were studied by theoretical conformational analysis. The potential energy of the system is chosen as the sum of non-valence, electrostatic and torsion interactions and the energy of hydrogen bonds. The low-energy conformations of molecules, the dihedral angles of the main and side chains of amino acid residues that make up the molecule were found, and the energy of intra- and interresidual interactions was estimated. It is shown that the spatial structure of the lactoferroxin A molecule is represented by fourteen forms of the main chain, and the spatial structure of the lactoferroxin B molecule by eleven forms of the main chain. Comparison of the obtained low-energy conformations of lactoferroxins A and B shows that they have quite a lot in common. In a small energy range of 0–3,0 kcal/mol, these molecules have many conformations. Therefore, it is precisely this that explains the fact that both molecules perform a common biological function. It can be assumed that tyrosine amino acid residues are involved in the performance of the biological function. In similar conformations, their side chains in space are approximately in the same positions. The results obtained can be used to elucidate the structural and structural-functional organization of lactoferroxin molecules.

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“…Нами были исследованы структурно-функциональные организации опиоидных пептидов энкефалинов, эндорфинов, эндоморфинов, динорфинов, неоэндорфинов, адренорфина, а в настоящее время исследуется пространственная структура экзорфинов. Эта работа является продолжением наших предыдущих исследований [4][5][6][7][8][9][10][11][12].…”

unclassified

Three-Dimensional Structure of the Beta-Lactorfin Molecule

Agayeva

¹

,

Abdinova

²

,

Akhmedova

³

et al. 2022

Russian Journal of Biological Physics and Chemisrty

0

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Opioid peptides cause pain relief, sedation and sleep, as well as a euphoric state and a number of autonomic reactions. These peptides are of animal and plant origin. A number of exogenous peptides obtained from food have opiate-like properties. This peptides were named exorphins. The discovery of the opioid activity of the peptide components of food has led to the assumption that certain types of food can act on the central nervous system like opiate drugs. A number of milk exorphins have been found that have opioid receptor antagonist properties. These include casoxins A, B, C, human casoxin D, as well as lactoferroxins A, B and C, as well as alpha and beta lactorphins. The possibility of the formation of these peptides during the hydrolysis of the corresponding proteins by peptidases of the gastrointestinal tract has been proven in vitro. Representatives of exorphins are also cytochrophins and hemorphins. It is assumed that these peptides can be formed in vivo during the proteolytic cleavage of cytochrome b and hemoglobin. The beta-lactorphine molecule is a representative of this class. The conformational possibilities of the beta-lactorphine Tyr-Leu-Leu-Phe molecule were studied by the method of theoretical conformational analysis. The potential function of the system is chosen as the sum of non-valence, electrostatic and torsion interactions and the energy of hydrogen bonds. The low-energy conformations of the alpha-lactorphine molecule, the values of the dihedral angles of the main and side chains of the amino acid residues that make up the molecules were found, and the energy of intra- and interresidual interactions was estimated. It has been shown that the spatial structure of the beta-lactorphine molecule can be represented by eight forms of the main chain. The results obtained can be used to elucidate the structural and structural-functional organization of exorphin molecules.

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The Spatial Structure of the ACTH-(7–10) Molecule

Cited by 7 publications

References 2 publications

Structural Organization of Soymorphin Molecules

Structural Organization of Soymorphin Molecules

Structural Organization of Lactoferroxin Molecules

Three-Dimensional Structure of the Beta-Lactorfin Molecule

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