We are excited to present the following speakers scheduled to deliver seminars at the symposium. The speakers were selected and invited based on providing a diverse range of topics in effort to make the symposium as applicable and interesting to as many people as possible. *Synopses are taken directly from provided information.

Dr. Michelle C. Chang - University of California Berkeley

Assistant Professor of Chemistry

Ph.D. Massachussetts Institute of Technology

Research Website

Building new chemical function in living organisms

Living systems have evolved the capacity to carry out many chemical transformations of interest to synthetic chemistry if they could be redesigned for targeted purposes. However, our ability to mix and match enzymes to construct de novo pathways for the cellular production of small molecule targets is limited by insufficient understanding how chemistry works inside a living cell. Our group is interested in using synthetic biology as a platform to study how enzymes function in vivo and to use this understanding to build new synthetic pathways for the production of pharmaceuticals, nanomaterials, and fuels using living cells.


Dr. Sonya Franklin - Monsanto
 

 

Director of Enabling Technologies, Monsanto Co.
Former Director of Protein Technologies, Monsanto Co.
Former Associate Professor of Chemistry, University of Iowa

Postdoc, Bioinorganic Chemistry, California Institute of Technology
Ph.D. , Chemistry, University of California - Berkley

Website

 

Engineering proteins to improve biological function: Applications of Ag Biotech

Advances in the field of molecular biology over the last 30 years have greatly enabled our ability to modify the structure, stability and activity of proteins of interest. The growth of this "protein design" discipline has resulted in the modification of numerous proteins resulting in beneficial therapeutic agents, biochemical reagents, and even enhanced agricultural crops. This talk will highlight advances in protein design as it relates to agricultural applications.


Daniel A. Harki - University of Minnesota

Assistant Professor, Department of Medicinal Chemistry

Postdoc, California Institute of Technology
Ph.D., Pennsylvania State University

Research Website

Semisynthetic parthenolide analogues: Chemical probes and anticancer agents

Parthenolide (PTL) is a plant-derived natural product from feverfew and a well-established active component of many natural medicines. Recent discoveries that PTL targets cancer stem cell populations in multiple human cancers have sparked significant interest in developing PTL for applications in cancer chemotherapy. To elucidate the mechanism of cancer stem cell toxicity by PTL, which is not curently established, we have developed PTL-based chemical probes for utilization in protein pull-down and identification experiments. We have also synthesized a small library of PTL-inspired analogues to optimize PTL for enhanced potency, specificity, and water solubility. Our progress in both areas will be presented.


Dr. Kim D. Janda - The Scripps Research Institute

Director, The Worm Institute of Research & Medicine, The Scripps Research Institute
Professor, Departments of Chemistry, Chemistry & Immunology, and Microbial Science, The Scripps Research Institute
Skaggs Scholar, The Skaggs Institute for Chemical Biology, The Scripps Research Institute
Ely R. Callaway Jr., Chair in Chemistry, The Scripps Research Institute

Postdoc (Molecular Biology), Research Institute of Scripps Clinic
PhD (Organic Chemistry), University of Arizona

Research Website

Interfacing chemistry and biology to discover molecules with function

Nature, and in particular biology, contains information to instruct scientists about what is possible. This can serve as an inspiration to probe the frontiers of biology-chemistry. At the same time, chemistry can contribute to our understanding of biology and also to our ability to manipulate complex systems for human health and welfare. The combination of the tools and principles of chemistry, together with the tools of modern molecular biology, allows us to create complex synthetic and natural molecules, and processes with novel biological, chemical and physical properties. This lecture will illustrate the tremendous opportunities that lie at this interface of biology, chemistry and medicine by describing a number of examples that we are actively working on in our laboratory.


Michael Mbuguni - University of Minnesota

 

Ph.D Candidate (with John. D. Lipscomb)
Department of Biochemistry, Molecular Biology, and Biophysics
B.S., University of Wisconsin - Eau Claire

Research website

Oxygenated intermediates from Homoprotocatechuate 2,3 Dioxygenase (2,3-HPCD)

The binding of O2 to mononuclear non-heme Fe(II) enzymes to yield a Fe(III)-O2·-intermediate has been proposed for many enzymes, but few such species have been characterized. As such, we have used the Fe(II) dependent Extradiol Dioxygenase 2,3-Homoprotocatechuic Dioxygenase (or 2,3-HPCD) to study the mechanism of O2 activation by mononuclear non-heme Fe(II) enzymes. In nature, Extradiol Dioxygenases catalyze the O2 dependent ring-opening reaction of catecholic substrates, allowing aerobic microorganisms to metabolize naturally occurring and man-made aromatic compounds. Using Stopped-Flow spectroscopy, Rapid Freeze-Quench techniques together with Electron Paramagnetic Resonance and Mössbauer spectroscopies, we have studied for the first time, the electronic structure of a non-heme Fe(III)-O2·- complex from an active site mutant of 2,3-HPCD. This effort has also resulted in observation and characterization of oxygenated reaction intermediates observed when wild-type 2,3-HPCD and it’s active site mutants react with the native substrate Homoprotocatechuic acid (HPCA) and O2. Our results illustrate facile electron transfer between FeII, O2, and the catecholic substrate HPCA, supporting the proposed mechanism for the wild-type enzyme.