Serine proteinases, a class of proteolytic enzymes, play critical roles in numerous physiological processes including blood coagulation, fibrinolysis, development, and various pathological states (pulmonary emphysema, tumor invasion, metastasis, inflammation).
Low-molecular-weight synthetic inhibitors of serine proteinases may be useful to supplement deficient natural macromolecular inhibitors. Suicide substrates (or mechanism-based inactivators) that generate reactive species at the active site of target enzymes are potentially very selective.
New dihydrocoumarine derivatives incorporating a latent functionality have been designed. Previously, some compounds of this class have shown good inhibitory potency as mechanism-based inactivators.
In a preliminary study, different newly synthesized dihydrocoumarines were checked as inhibitors of various serine proteinases. A further pharmacomodulation would increase their biological recognition.