PHYSICS & SPACE SCIENCES
BAKU STATE UNIVERSITY JOURNAL of
PHYSICS & SPACE SCIENCES
ISSN: 3006-6123 (ONLINE);     
Structural organization of lactoferroxine C
Received: 11-Oct-2024 Accepted: 01-Nov-2024 Published: 16-Dec-2024 Download PDF
Leyla N. Agayeva; Afiyat A. Abdinova; Simnara R. Akhmedova; Nijat F. Akhmedov
Abstract
A number of exogenous peptides derived from nutrients have opioid-like properties. Lactoferroxine is a glycoprotein present in milk and small amounts in exocrine fluids such as bile and tears. The conformational capabilities of the lactoferroxine C molecule (H-Lys1-Tyr2-Leu3-Gly4-Pro5-Gly6-Tyr7-OH) have been studied by the method of theo-retical conformational analysis. The potential function of the system is chosen as the sum of non-bonded, electrostatic, torsion interactions and the energy of hydrogen bonds. Low-energy conformations of the lactoferroxine molecule and the dihedral an-gles of the main and side chains of amino acid residues included in the molecule were found, the energy of intra-and intersubstance interactions was estimated. It has been shown that the spatial structure of the lactoferroxine molecule is represented by eight structural types. It can be assumed that the molecule performs its physiological func-tions in these structures. These three-dimensional structures make it possible to pro-pose synthetic analogs for a given molecule. The results obtained can be used to eluci-date the structural and structure-functional organization of humen casomorphin mole-cule.

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