• Publications
  • Influence
Unnatural amino acids increase activity and specificity of synthetic substrates for human and malarial cathepsin C
TLDR
This study presents a new approach with a tailored fluorogenic substrate library designed and synthesized to probe the S1 and S2 pocket preferences of these enzymes with both natural and a broad range of unnatural amino acids, which resulted in the design of significantly better substrates than those previously known.
Stereoselective synthesis of 1-aminoalkanephosphonic acids with two chiral centers and their activity towards leucine aminopeptidase.
TLDR
Simultaneous deprotection and oxidation by the action of bromine water provided equimolar mixtures of the RS:RR and SR:SS diastereomers of desired acids that appeared to act as moderate inhibitors of kidney leucine aminopeptidase with potency dependent on the absolute configuration of both centers of chirality.
Structure-Guided, Single-Point Modifications in the Phosphinic Dipeptide Structure Yield Highly Potent and Selective Inhibitors of Neutral Aminopeptidases
TLDR
Seven crystal structures of alanyl aminopeptidase from Neisseria meningitides complexed with organophosphorus compounds were resolved to determine the optimal inhibitor–enzyme interactions, and novel contacts, which were promising for inhibitor development, were identified.
The influence of α-aminophosphonic acids on the activity of aminopeptidase from barley seeds—an approach to determine the enzyme specificity
TLDR
Inhibitory potencies of 24 α-aminophosphonic acids against barley seeds have been determined and the enzyme was sensitive mostly to the influence of phosphonic acid analogues of phenylalanine and its homologues, thus showing narrow specificity if compared with porcine aminopeptidases M1 and M17.
Pentapeptides containing two dehydrophenylalanine residues ‐ synthesis, structural studies and evaluation of their activity towards cathepsin C
TLDR
Results of molecular modeling suggested significant difference between peptides, depending of the type of amino acid residue in position 5 in peptide chain, may act as competitive slow‐reacting substrates and therefore exhibit inhibitory‐like properties.
...
...