cGMPnin

cGMPnin, also known as cyclic guanosine monophosphate (cGMP) non-enzymatic inhibitor, is a small molecule that inhibits the activity of soluble guanylyl cyclase (sGC). sGC is an enzyme that catalyzes the conversion of guanosine triphosphate (GTP) to cyclic guanosine monophosphate (cGMP), a second messenger molecule involved in various cellular processes, including smooth muscle relaxation and platelet aggregation.

cGMPnin was first identified in the venom of the snake Bothrops jararaca. It is a potent inhibitor of sGC, with an IC50 value in the nanomolar range. The structure of cGMPnin is unique, featuring a bicyclic guanosine moiety and a guanidine group, which are essential for its inhibitory activity.

The mechanism of action of cGMPnin involves the binding to the heme iron of sGC, leading to the inhibition of GTP binding and subsequent cGMP production. This inhibition results in the disruption of downstream signaling pathways, leading to various physiological effects, such as vasoconstriction and platelet aggregation.

cGMPnin has been studied for its potential therapeutic applications, particularly in the treatment of cardiovascular diseases. Its ability to inhibit sGC and disrupt downstream signaling pathways makes it a promising candidate for the development of new drugs. However, further research is needed to fully understand its pharmacological properties and potential side effects.

In summary, cGMPnin is a potent inhibitor of soluble guanylyl cyclase, with potential therapeutic applications in cardiovascular diseases. Its unique structure and mechanism of action make it an interesting target for further research and drug development.