The Influence of Non-Protein Amino Acids and Peptides on Bacterial Collagenase

Abstract

Bacterial collagenolytic proteases have drawn increasing attention due to their essential role in the global nitrogen cycling and their virulent role in some diseases. The inhibition of these enzymes is attractive, as it does not attack the pathogen directly but rather blocks the colonization and infiltration of the host by the clostridia. Optically active non-protein α-amino acids have been screened for their ability to inhibit collagenase of Clostridium histolyticum. Both structure-based drug design approach (modeling) and that of determining enzyme activity in the presence of amino acids have been used to identify low molecular weight inhibitors of collagenase. The compounds able to inhibit collagenase activity have been revealed and IC50 values have been estimated.

A Stereoselective Entry to Enantiopure (S)-2-Amino-2-methyl-5-arylpent-4-ynoic Acids and Evaluation of Their Inhibitory Activity against Bacterial Collagenase G

“…A typical synthesis requires an excess of amino acids, coupling reagents and base to achieve high conversion at each step. Moreover, the synthesis of hydrophobic peptides poses additional challenges since aggregation of growing peptide chains is a common issue [41][42][43][44]. Given the importance of peptides, it is highly desirable to elaborate routes for the synthesis of new peptides.…”