Spring 2013
Weekly Chemistry Seminar-Matt Bogyo, Stanford University
February 8, 2013 3:00 PM – 4:00 PM
Druckenmiller Hall, Room 020
Proteases are enzymes that primarily function by degrading protein substrates. Since this process is irreversible, proteases must be carefully regulated within cells and organisms in order to prevent undesired consequences. Furthermore, proteases often pathogenic roles in common human diseases such as cancer, asthma, arthritis and atherosclerosis. Over the past decade, my laboratory has developed a series of small molecule probes that specifically bind to the active form of protease targets through an enzyme catalyzed chemical reaction. These reagents freely penetrate cells and can be used to enrich complex proteomic samples for monitoring of global patterns of protease activity as well as to directly image protease activity in live cells and whole animals. They can also be used to monitor the efficacy and selectivity of small molecule protease inhibitor drugs. We are currently applying these probes to study the role of specific proteases in the process of angiogenesis and metastasis in mouse models of cancer as well as during the process of inflammation in mouse models of atherosclerosis and asthma. In addition we have developed probes that bind proteases associated with the process of programmed cell death (apoptosis). These reagents allow the direct non-invasive imaging of cell death in vivo. We are currently developing these tools to further study the cell biology of tumor response to chemotherapy. Recent advances in these projects will be presented
Seminar: The micro- and macro-evolution of speciation: tales from tropical seas
February 13, 2013 4:00 PM – 5:00 PM
Druckenmiller Hall, Room 020
Seminar: The asthma epidemic: a challenge of applied immunology
February 14, 2013 4:00 PM – 5:00 PM
Druckenmiller Hall, Room 020
Weekly Chemistry Seminar-Lauren Buchanan, University of Wisconsin-Madison
February 15, 2013 3:00 PM – 4:00 PM
Druckenmiller Hall, Room 020
Amyloid fiber formation is associated with more than twenty diseases, including type 2 diabetes and Alzheimer's disease. Thus, there is great interest in developing amyloid inhibitors as potential therapeutics, but rational drug design is hindered by the dearth of detailed information about the structure and aggregation mechanism of amyloid fibers. Our group uses 2D IR spectroscopy with isotope labeling to study amyloid peptides and drug binding with residue-level structural specificity. I will introduce the method behind our spectroscopic technique and show how it has been applied to study hIAPP, the peptide implicated in type-II diabetes. Our results provide significant insight into the aggregation mechanism of hIAPP and experiments with a novel macrocyclic peptide inhibitor suggest a new approach to designing amyloid inhibitors.
Seminar: Species interactions in a changing ocean: sponge symbioses as models for understanding
February 18, 2013 4:00 PM – 5:00 PM
Druckenmiller Hall, Room 020
Weekly Chemistry Seminar-George O'Doherty, Northeastern University
February 22, 2013 3:00 PM – 4:00 PM
Druckenmiller Hall, Room 020
My research group has been working in two related areas of organic synthesis: carbohydrate synthesis and natural product synthesis. The unifying theme that connects our research in these two areas is our method of synthesis (asymmetric catalysis) and target selection (anti-cancer/anti-microbial agents). A recurring theme in the group's synthetic approaches to both types of targets is our reliance on asymmetric catalysis for the control of asymmetry. Fundamental to our approach is the development of highly efficient routes that transform, via catalysis, inexpensive achiral starting materials into enantiopure products, which are poised for the conversion into complex molecules with biologically relevant properties (i.e. enantioselective synthesis of a new “chiral pool” via asymmetric catalysis). Recently, we have found that these approaches have matured to the point where we have developed enantioselective routes to these complex molecules in sufficient quantities that are amenable for biomedical investigations.
Seminar: Physical and biological drivers of resource provisioning in coastal marine ecosystems
February 25, 2013 4:00 PM – 5:00 PM
Druckenmiller Hall, Room 020
Weekly Chemistry Seminar, David Forbes, University of South Alabama
March 1, 2013 3:00 PM – 4:00 PM
Druckenmiller Hall, Room 020
Reaction of sulfur ylide with aldehyde, imine, and ketone functionality affords the desired three-membered heterocycle in excellent yield. The sulfur ylide is generated in situ upon decarboxylation of carboxymethylsulfonium betaine functionality. Of the carboxymethylsulfonium betaine derivatives surveyed, the highest level of conversion of p-acceptor to heterocycle was obtained with the one having S-methyl and S-phenyl functionality bound to a thioacetate derivative. Methylene aziridinations and epoxidations involving the decarboxylation of carboxymethylsulfonium betaine functionality complements existing technologies with the advantages of the reaction protocol, levels of conversion, and scope. Presented will be our approach and application of methylene transfers using sulfur ylide technologies
Seminar: Centering the genome: molecular control of mitotic chromosome movements
March 7, 2013 4:00 PM – 5:00 PM
Druckenmiller Hall, Room 020
Welcome to the Chemistry Major
March 29, 2013 12:30 PM – 1:30 PM
Druckenmiller Hall, Room 004
Welcome to Chemistry
Weekly Chemistry Seminar-Tim Jackson,University of Kansas
April 19, 2013 3:00 PM – 4:00 PM
Druckenmiller Hall, Room 020
Weekly Chemistry Seminar-Jerry Meyer, Johns Hopkins University
April 26, 2013 3:00 PM – 4:00 PM
Druckenmiller Hall, Room 020
Weekly Chemistry Seminar-Dr. Amelia Fuller, Santa Clara University
May 3, 2013 3:00 PM – 4:00 PM
Druckenmiller Hall, Room 020