In this article, they are trying to find compound derivatives that can inhibit matrix metalloproteases by binding to the active site, effectively blocking them from performing their function. They characterized the inhibiting behavior of TPA, one of the most effective inhibitors, and found that upon diluting the enzyme off its inhibitor, that binding is reversible.
They then followed to investigate whether derived compounds of of TPA could induce similar effects on a variety of metalloproteases, both human and bacterial. They found varying results, with some compounds working better than others.
They then followed with docking analysis in which, through bioinformatic means, they try to describe the physical conformation of the inhibitor in the catalytic site of the protease and how it impeded activation. These results yielded key information of allosteric interactions that are key for correct binding, as well as which residues seem to have better inhibition than others.
Citations:
Rahman, F. et al. “Zinc-chelating compounds as inhibitors of human and bacterial zinc metalloproteases”. Molecules. 2021 Dec 22; 27(1):56.
https://pubmed.ncbi.nlm.nih.gov/35011288/