The first area focuses on mechanistic study of and inhibitor design for biologically important and mechanistically intriguing enzymes. We are currently studying the bacterial enzymes LuxS and S-adenosyl-homocysteine nucleosidase, which play pivotal roles in bacterial quorum sensing, biofilm formation, virulence regulation, and metabolism. Absent in humans, these enzymes are attractive targets for anti-infective agent development. Furthermore, we are striving to discover novel signaling molecules in bacterial communication.
The second area involves proteomic analysis and biochemical characterization of protein post-translational modifications and selective derivatization of proteins. More specifically, we are interested in protein methylations. S-Adenosyl-methionine (AdoMet)-dependent methylations result in a myriad of crucial biological functions. For example, abnormal methylation has been associated with tumor progression, arthritis, depression, and possibly cardiovascular diseases. We are devising new methods to detect and quantify such modifications. Additionally, we are developing robust colorimetric assays for methyltransferases, which allows screening for novel methyltransferase activities as part of our effect in functional proteomics research. We are also interested in small molecule methylation, particularly the effects on the metabolism of drugs and xenobiotics in humans.
Research opportunities are available for postdoctoral fellows, undergraduate and graduate students. A wide spectrum of techniques are applied in our research, including organic synthesis, drug design, protein expression and purification, enzyme assay and inhibitor screening, protein chemistry and mass spectrometry. Contact Sunny by email.