Metabolites Isolated from Sch. Bip and Their Synthesized Oximes Inhibit Angiotensin I-Converting Enzyme Activity in Vascular Smooth Muscle.

Angiotensin-Converting Enzyme (ACE) plays a pivotal role in the renin-angiotensin system, modulating blood pressure and electrolyte homeostasis by deactivating bradykinin and activating angiotensin II. Metabolites from ( and ), a plant indigenous to the Andean region of the Atacama Desert, and their respective oximes, and , were subjected to molecular docking analysis, employing six ACE crystal structures. ACE activity assays revealed that oximes exhibited superior inhibitory effects compared to metabolites. Among the compounds investigated, emerged as the most potent ACE inhibitor ( = 11.5 μM and = 13.4 μM). The vascular contractile response to Angiotensin I showed significant ( < 0.05) reductions in Ang I contraction with , , and (97 ± 6%, 81 ± 6%, 81 ± 3% compared to control), while exhibited no such effect. These results reinforce the potential of as a promising ACE inhibitor and highlight its impact on vascular contractility. As such, it is a promising candidate for ACE inhibition and hypertension treatment.