Targeted synthesis of N-tertbutoxycarbonylglycyl-(S)-α-allylglycyl-(S)-alanine tripeptide and study of its effect on collagenase activity

The 10 new peptides have been constructed on the basis of (S)-α-allyl-glycine (2-aminopent-4-enovic acid) non-protein amino acid by ChemOffice software. To study their possible interaction with collagenase enzyme, molecular docking program – AutoDockVina software was used. Analyzing the obtained results, N-t-BOC-Gly-(S)-α-allylGly-(S)-Ala tripeptide was identified by maximum values of Gibbs free energy (ΔG=-6.2 kcal/mol) and minimum values of dissociation constant (KD=0,28532μmol) of ligand-macromolecular interaction. The synthesis of a new undescribed in the literature N-t-BOC-Gly-(S)-α-allylGly-(S)-Ala tripeptide has been carried out by the activated ester method. In vitro study of the synthesized tripeptide effect on the activity of collagenase enzyme at various peptide concentrations has been carried out, as a result of which it has been found out that the inhibition of the enzyme is 41.06% at 0.8989 mmol/l concentration of the synthesized tripeptide