Final answer:
Activated matrix metalloproteinases, like collagenase, can be rapidly inhibited by selective irreversible covalent inhibitors that target their active sites, including Peptidyl Michael acceptor inhibitors and vinyl sulfones. Some of these inhibitors are stable and have even entered clinical trials.
Step-by-step explanation:
Activated matrix metalloproteinases (MMPs), like collagenase, can be rapidly inhibited by various means. Some of the most effective inhibitors are selective irreversible covalent inhibitors tailored to target the active sites of these proteases. For instance, cysteine proteases can be inhibited by Peptidyl Michael acceptor inhibitors or vinyl sulfones and α,β-unsaturated carbonyl derivatives which form covalent bonds with the proteases' active sites. Such inhibitors are designed to be stable and require the catalytic machinery of the proteases for activation, offering a tailored approach to blocking the activity of specific proteases. These inhibitors have even progressed to clinical trials, exemplifying their potential in therapeutic contexts.