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Objective Soluble guanylyl cyclase, (sGC) is an enzyme that can be activated endogenously by nitric oxide (NO). As its particulate counterparts, the role of the cytoplasmic sGC inside the cell is to convert GTP to the second messenger, cGMP. NO is produced by nitric oxide synthase during the conversion of l-arginine to l-citrulline. NO binds to the ferrous heme of sGC and activates the enzyme, augmenting the production of cGMP which leads to the activation of cGMP-dependent targets. The activation of various proteins through elevated cGMP production by sGC produces physiological functions like vasodilation, inhibition of platelet aggregation, photosensitivity, and cell growth. However, studies have indicated that during pathophysiological conditions like sepsis and cancer, the inhibition of sGC activity could potentially be beneficial in achieving a desired cellular and pharmaceutical response. In addition, a common inhibitor of sGC, ODQ, only inhibits NO-stimulated sGC, not basal, and ODQ also does not work well under high NO concentrations thus furthering the need to develop novel sGC inhibitors.

Identification of new inhibitors of soluble guanylyl cyclase activity