Baku, Azerbaijan
The opioid peptides are currently considered as the most studied group of peptide signaling substances. The opium causes the pain relief, sedation and falling asleep, as well as a euphoric state and a number of vegetative reactions. The opioid peptides are of animal and plant origin. A number of exogenous peptides derived from food have opioid-like properties. Such peptides were called exorphins. The conformational capabilities of exorphin A4 and A5 molecules were studied by the method of theoretical conformational analysis. 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 these peptides are found, the values of the dihedral angles of the main and side chains of amino acid residues forming them, the energy of intra-and interactions are estimated. It is shown that the spatial structure of the investigated molecules can be represented by eight conformations. The obtained results can be used to clarify the structural and structural-functional organization of the exorphin molecules.
exorphin, opioid, structure, conformation
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