The Connection Between Structure Modification and Anti-Inflammatory Effects of Prolyl-Glycyl-Proline (PGP)

• Published in: International journal of peptide research and therapeutics 2018-09, Vol.24 (3), p.347-353
• Main Authors: Kurenkova, A. D., Andreeva, L. A., Umarova, B. A., Gavrilova, S. A., Myasoedov, N. F.
• Format: Article
• Language: English
• Subjects: Amino acid sequence; Animal Anatomy; Biochemistry; Biomedical and Life Sciences; Compound 48/80; Glycine; Histamine; Histology; Inflammation; Life Sciences; Lipopolysaccharides; Mast cells; Molecular Medicine; Morphology; Peptides; Permeability; Pharmaceutical Sciences/Technology; Pharmacology/Toxicology; Polymer Sciences; Proline; Secretion; Skin
• ISSN: 1573-3149; 1573-3904
• DOI: 10.1007/s10989-017-9619-z

It has previously been shown that many of the peptides that contain proline and glycine amino acids have a pronounced physiological activity, however, the amino acid sequence, which to the greatest extent determines their properties, remains unknown. In this paper, we studied the effect of modified forms of the Prolyl-Glycyl-Proline (PGP) peptide on the secretion of histamine from isolated mast cells and the permeability of vessels in the skin of rats after intradermal administering of Synacthen, lipopolysaccharide LPS and compound 48/80. We have shown that peptides Semax, Selank, PGPL FPG, GPG, PG and GP reduced the secretion of histamine from mast cells and increased the vascular permeability after the administration of Synacthen and LPS, but not compound 48/80. At the same time peptides PLP, PGA and RGP had no effect on these parameters. Thus, the structural modification of PGP affects its properties only if a glycine or proline is replaced by another amino acid.