HS6ST2 Inhibitors

Chemical inhibitors of HS6ST2 can exert their inhibitory effects through various biochemical interactions and mechanisms. Suramin, for instance, has a broad-spectrum ability to bind to multiple growth factor receptors and enzymes, including sulfotransferases like HS6ST2. By directly binding to the active site or substrate binding site of HS6ST2, Suramin can obstruct the enzyme's normal function, which is essential for transferring sulfate groups to its substrates. Similarly, Triclosan is known for its inhibitory effects on enoyl-acyl carrier protein reductase, and it can also extend this inhibition to other sulfotransferases by interacting with their active sites, leading to the functional inhibition of HS6ST2. Bisphenol A, acting as an endocrine disruptor, can bind to various enzymes and potentially interfere with the enzyme-substrate interactions of HS6ST2, thereby inhibiting its sulfation activity.

Additionally, several polyphenolic compounds exhibit inhibitory actions on protein kinases, which can indirectly inhibit HS6ST2. Flavonoids like Quercetin, Kaempferol, and Genistein, as well as polyphenols like Resveratrol, have the capacity to bind to protein kinases, which could in turn alter the phosphorylation state of HS6ST2 or its substrates, thus affecting HS6ST2's enzymatic activity. Curcumin, known to inhibit a variety of protein kinases, can similarly influence HS6ST2 by changing the phosphorylation patterns of the protein itself or its related proteins. Chlorogenic acid and Ellagic acid, by acting on various enzymes, could interact with the active site or allosteric sites of HS6ST2, potentially inhibiting its function. Catechins like Catechin and Epigallocatechin gallate (EGCG) are known enzyme inhibitors that can engage directly with HS6ST2, preventing its sulfotransferase activity, thereby leading to the loss of its functional capacity to catalyze the transfer of sulfate groups to its specific substrates.