PLENARY KEYNOTE PROGRAM

The Drug Discovery Chemistry event is a dynamic conference for medicinal and biophysical chemists working in pharma and biotech. It is one of the few international events focused solely on discovery and optimization challenges of small molecule drug candidates.

Drug Discovery Chemistry offers a plenary keynote session on Tuesday, April 2 from 4:20 - 5:15 pm PDT and Thursday, April 4 from 8:30 - 9:20 am PDT. Join hundreds of your colleagues during each of these presentations, which include live Q&As with the audience.

PLENARY KEYNOTE SESSION - TUESDAY AFTERNOON

Barry Sharpless, PhD4:30 pm Applications of SuFEx Click Chemistry for Drug Discovery and Chemical Biology
Barry Sharpless, PhD, Professor, Chemistry, Scripps Research Institute; 2022 and 2001 Nobel Laureate
My work has been guided by the modular simplicity of nature—the fact that all molecules of life are made from several dozen building blocks. Here I will discuss the Sulfur(VI) Fluoride Exchange (SuFEx), a second near-perfect click chemistry reaction pioneered here at Scripps. SuFEx allows reliable molecular connections to be made under metal-free conditions. I will include applications in drug discovery, chemical biology, and polymer chemistry.

Dr. Sharpless's >50-year research career has been devoted to finding new tools and better general methods for exploring the chemical universe. He shared the 2001 Nobel Prize in Chemistry for his work on chirally catalyzed oxidation reactions. In 2022, Barry was awarded the Nobel Prize in Chemistry for developing 'click chemistry', making him only the second scientist to win two Nobels in Chemistry. Click chemistry, a discovery methodology based on the insight that the molecules of life are made from less than several dozen small building blocks, provides a reliable way to uncover useful chemical function and spring-loaded ‘perfect’ reactions.

Today the focus of the Sharpless lab is Sulfur(VI) fluoride exchange (SuFEx) click chemistry, which allows reliable molecular connections under metal-free conditions. SuFEx has applications in synthetic methodology; chemical biology and drug discovery; and polymers and material science. Barry received his BA from Dartmouth College in 1963 and his PhD in Chemistry from Stanford University in 1968. Before joining Scripps Research in 1990, he was chemistry faculty at MIT and Stanford.

PLENARY KEYNOTE SESSION - THURSDAY MORNING

Daniel Nomura8:35 am Reimagining Druggability Using Chemoproteomic Platform
Daniel Nomura, PhD, Professor of Chemical Biology and Molecular Therapeutics, Department of Chemistry, University of California, Berkeley
One of the greatest challenges that we face in discovering new disease therapies is that most proteins are considered “undruggable,” in that most proteins do not possess known binding pockets or “ligandable hotspots” that small molecules can bind to modulate protein function. Our research group addresses this challenge by applying chemoproteomic platforms to discover and pharmacologically target unique and novel ligandable hotspots for disease therapy.

Dan Nomura is a professor in the Departments of Chemistry, Molecular and Cell Biology, and Nutritional Sciences and Toxicology at the University of California, Berkeley and an adjunct professor in the Department of Pharmaceutical Chemistry at UCSF. He is also the director of the Novartis-Berkeley Center for Proteomics and Chemistry Technologies and an Investigator in the Innovative Genomics Institute. He earned his BA in Molecular and Cell Biology and PhD in Molecular Toxicology at UC Berkeley with Professor John Casida and was a postdoctoral fellow at The Scripps Research Institute with Professor Ben Cravatt before returning to Berkeley as a faculty member in 2011. Among his honors are selection as a Searle Scholar, American Cancer Society Research Scholar Award, the Department of Defense Breakthroughs Award, and the Mark Foundation for Cancer Research ASPIRE Award. The Nomura Research Group is focused on redefining druggability using chemoproteomic platforms to tackle the undruggable proteome.