![Innovative Enzymology]()
Hundreds of FDA-approved drugs are inactivated in the body through sulfonation--a process carried out by sulfotransferases (SULTs) — these enzymes regulate the interactions between hundreds, if not thousands, of small signaling molecules and their receptors in human cells. Preventing sulfonation without compromising SULTs’ essential functions has proven challenging. Using a novel molecular design strategy, Thomas Leyh, Ph.D., and his research team have demonstrated that it is possible to prevent the sulfonation of a compound without inhibiting SULTs or significantly altering the interaction of the compound with its receptor. Using this approach, Dr. Leyh and colleagues increased, by four orders of magnitude, the efficacy of a Raloxifene-based estrogen receptor agonist. The work demonstrates that it is now possible to control the sulfonation of a single compound in the body. It also highlights the significant potential of the technique for enhancing the efficacy of sulfonated drugs, and for exploring sulfuryl-transfer biology. The findings are reported in the “Featured Research Article” in the May 19 issue of Cell Chemical Biology. Its lead author is Ian Cook, Ph.D., a postdoctoral fellow in the Leyh lab. The journal’s website features images from the research, under the “Free Featured Articles” section. Dr. Leyh is a professor of microbiology & immunology.
Posted on: Tuesday, June 07, 2016