UST Inhibitors

UST inhibitors encompass a diverse group of chemicals that primarily function by hampering the sulfation processes vital for glycosaminoglycan biosynthesis. These chemicals either directly impede UST activity or act on closely related pathways that indirectly influence UST function. The primary strategy employed by these inhibitors is to obstruct the binding or the activity of the universal sulfo group donor, PAPS. Suramin, for instance, is known to compete with PAPS, and PAP, being the immediate substrate for sulfotransferases, can in elevated concentrations act as a feedback inhibitor.

Furthermore, the sulfation process, which is a fundamental aspect of UST's function, is perturbed by compounds like chlorate and sodium perchlorate. By competing with sulfate, these inhibitors ensure that the sulfotransferase activity is compromised. Another approach to achieve inhibition is through structural mimicry. PAPS analogues and sulfate analogues have been crafted in a manner where they closely resemble their native counterparts, ensuring they can compete with and disrupt UST's typical interactions. Other inhibitors such as ozarelix, quercetin, and bosentan, while not exclusive to UST, do impact sulfotransferase functions, thus indirectly modulating UST activity. Sodium salicylate, by affecting COX enzymes, is capable of indirectly disturbing the sulfation pathways. Lastly, compounds like DIDS and desipramine can affect a myriad of enzymatic pathways, including those involving sulfation.