Baku, Azerbaijan
Baku, Azerbaijan
The spatial structure of cardioactive nonapeptide molecule Pro-Phe-Cys-Asn-Ala-Phe-Tyr-Gly-Cys- NH2 (CCAP, Crustacean cardioactive peptide) and the conformational properties were investigated using molecular mechanics method. This peptide was first isolated from the pericardial organs of the shore crab Carcinus maenas. It is found in crustaceans and insects where it behaves as a cardioaccelerator, neuropeptide transmitter for other areas of the neurous system and a hormone. Crustacean cardioactive peptide is highly conserved, amidated cyclic nonapeptide with the primary structure PFCNAFTGC-NH2 and disulfide bridge between Cys3 and Cys9. The potential energy of the molecule was chosen as the sum of the non-valent, electrostatic and torsional interaction energies and the energy of hydrogen bonds. The 7 low-energy conformations of this molecule, the dihedral angles of the backbone and side chains of the amino acid residues of the tetrapeptide, and the energies of intra- and inter-residual interactions were determined. It is revealed that low energy conformations of this molecule have cyclic type of backbone. These folded forms bring parts of the backbone and the side chains of the amino acids together, and they result in convenient interactions.
nonapeptide, conformation, molecule, spatial structure
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