The spatial structure of the cardio active peptides

Akhmedov, N.; Abbasli, R.M.; Ismailova, L. I.

doi:10.1109/icaict.2009.5372609

Cited by 2 publications

(2 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Расчеты трехмерной структуры пептидных молекул позволяют определить геометрические и энергетические параметры пептидов, значения двугранных углов основной цепи и боковых цепей аминокислот, входящих в молекулу, а также энергетические вклады внутримолекулярных взаимодействий. Данная работа является продолжением исследований пространственного строения пептидных молекул [9][10][11][12][13][14].…”

Section: ключевые слова: молекула пространственная структура пентапеп...unclassified

Threedimensional Structure of the Pentapeptide Molecule Arg-Glu-Arg-Gly-Pro

Ismailova

Abbasli

Akhmedov

2022

Russian Journal of Biological Physics and Chemisrty

View full text Add to dashboard Cite

It seems relevant to carry out structural and functional studies of glyprolines and their synthetic analogues on model systems using theoretical research methods. Glyprolines are a family of short peptides whose amino acid sequences contain residues of proline and glycine. Currently their mechanisms of action are poorly understood. Great interest in their structure is caused by the possibility of creating new drugs that are the human body’s own reserve. Glyproline molecules are stable and eddicient. Using the method of molecular mechanics, the spatial structure and conformational properties of the glyproline pentapeptide molecule Arg-Glu-Arg-Gly-Pro were determined. The potential energy of the molecule was estimated as the sum of non-valent, electrostatic, torsion interactions and the energy of hydrogen bonds. 9 low-energy conformations were found for glyproline pentapeptide, the values of structure the dihedral angles of the main and side chains, and the energy of intra-and inter-residue interactions was estimated. It is revealed that low energy conformations of this molecule have the half-folded type of backbone. The side chains of the Arg and Glu amino acids in low-energy conformations carry out effective interactions and are conformationally labile amino acids, they bring together the regions of the main chain and the side chains of the amino acids included in the pentapeptide.

show abstract

Section: ключевые слова: молекула пространственная структура пентапеп...unclassified

Threedimensional Structure of the Pentapeptide Molecule Arg-Glu-Arg-Gly-Pro

Ismailova

Abbasli

Akhmedov

2022

Russian Journal of Biological Physics and Chemisrty

View full text Add to dashboard Cite

show abstract

“…Для нахождения пространственного строения данной гексапептидной молекулы использовалась специально разработанная программа [8]. Данная научная работа является продолжением проведенных нами расчетов пространственной структуры пептидных молекул [9][10][11][12][13][14].…”

unclassified

Structural Organization of the Glyproline Hexapeptide Molecule

Ismailova,

Akhmedov

2024

Russian Journal of Biological Physics and Chemisrty

View full text Add to dashboard Cite

Computer modeling based on the use of the method of theoretical conformational analysis and programs that allow obtaining a graphic image of the spatial structures of biomolecules was performed for a hexapeptide molecule – glyproline H-Phe-Gly-Gly-Phe-Gly-Pro-OH. Glyprolines are short peptides whose amino acid sequences contain glycine and proline residues. Their mechanisms of action are currently poorly understood. Using the method of molecular mechanics, the spatial structure and conformational possibilities of this hexapeptide molecule were determined. Its potential energy was estimated as the sum of non-valente, electrostatic, torsion interactions and the energy of hydrogen bonds. 9 low-energy structures were found for the glyproline hexapeptide, the values of the dihedral angles of the main and side chains of the amino acids included in the molecule. The energy of intra- and interresidual interactions was estimated. The calculation showed that the folded forms of the main chain are low-energy for the hexapeptide. In them, the side chains of amino acids phenylalanine and proline, which are conformationally rigid, carry out effective interactions with all parts of the hexapeptide molecule.

show abstract

The spatial structure of the cardio active peptides

Cited by 2 publications

References 4 publications

Threedimensional Structure of the Pentapeptide Molecule Arg-Glu-Arg-Gly-Pro

Threedimensional Structure of the Pentapeptide Molecule Arg-Glu-Arg-Gly-Pro

Structural Organization of the Glyproline Hexapeptide Molecule

Contact Info

Product

Resources

About