Chemistry Newsblog

Dr. Donald Bergstrom
Professor Emeritus
Department of Medical Chemistry and Molecular Pharmacology,
Purdue University, West Lafayette, Indiana
Date: October 16, 2015
Place: Chem-Sci Room 101
Time: 3:00 pm

Abstract
For more than a half century I have designed and created new molecules. My research has been shaped within the contexts of culture, time, and place, at times responding to the work of others, but always attempting to ride the wave front of science. “At the End of Chemistry” follows the trajectory of my research from rocket design in the 1950’s to nanomaterials in the 21st century. It is both report and inquiry about the nature of research.

Biography
Don Bergstrom has held faculty positions at Purdue University (1989-2011), the University of North Dakota, and the University of California, Davis. He holds degrees in chemistry from the University of Washington (BS, 1965) and the University of California, Berkeley (PhD, 1970). From the early 1970s the work in his laboratory focused on nucleic acid chemistry, particularly the synthetic chemistry and applications of nucleosides. In the 21st century his efforts expanded into areas of nanotechnology and new approaches to drug design based on concepts of molecular self-assembly. He is currently a 2nd year graduate student in the MFA program in Applied Craft + Design at the Pacific Northwest College of Art.

Dr. Ayyalusamy Ramamoorthy, Professor
Biophysics and Department of Chemistry, University of Michigan
Date: September 25, 2015
Place: Chem-Sci Room 101
Time: 3:00 pm


Abstract
Membrane proteins are an exciting class of biomacromolecules and play important roles in a variety of biological processes that are directly linked to major diseases including cancer, aging-related diseases, and infectious diseases. A complete understanding of their function can only be accomplished using high-resolution structures and dynamics. In spite of recent developments in structural biology, membrane proteins continue to pose tremendous challenges to most biophysical techniques. A major area of research in my group is focused on the development of NMR techniques to study the dynamic structures of membrane bound proteins such as cytochrome b5, cytochrome P450 and cytochrome P450-reductase. In my talk, I will present strategies to study the structure and dynamics of these challenging systems and also on the electron transfer mechanism that enables the enzymatic function of P450. Atomic-level resolution NMR structures of amyloidogenic proteins revealing the misfolding pathway and early intermediates that play key roles in amyloid toxicity will also be presented.
References:
J. Biol. Chem. (2015) 290:12705-18; 290: 4843-55; 288:22080-95.
Chem. Soc. Rev. (2014) 43:6692-6700; J. Phys. Chem. Lett. (2014) 5:1864.

Biography
Dr. Ayyalusamy Ramamoorthy is Professor of Biophysics and Chemistry at University of Michigan, where he has been since 1996. He has applied NMR spectroscopy and other biophysical techniques to investigate high-resolution structure, dynamics, and functional properties of membrane proteins, amyloid proteins/peptides, and antimicrobial peptides. He has published more than 250 peer-reviewed papers in leading high impact journals like Science, PNAS, JACS, J. Biol. Chem., and Angew. Chem. Eng. Intl., written several review articles, edited 2 books on NMR spectroscopy, brought out several special issues as a guest editor, and organized several conferences related to NMR spectroscopy. He is a member of editorial boards of J. Biol. Chem., Plos One, Scientific Reports, Peer J, Biochimica Biophysica Acta, Journal of Magnetic Resonance, Chemistry and Physics of Lipids, Solid State Nuclear Magnetic Resonance Spectroscopy, and Magnetic Resonance in Chemistry. He has been a PI or co-PI on several NIH (and other) sponsored projects.
For more information visit http://rams.biop.lsa.umich.edu/

Dr. Xiaohu Xia
Assistant Professor
Department of Chemistry, Michigan Tech
September 18, 2015
Chem-Sci Room 101 3:00pm

Abstract
Peroxidase mimics (or artificial peroxidase) with dimensions at the nanoscale have received great interest as emerging artificial enzymes for biomedicine and environmental protection. While a variety of peroxidase mimics have been actively developed since 2007, limited progress has been made toward improving their catalytic efficiency. In our recent work (ACS Nano, 2015, in press, DOI: 10.1021/acsnano.5b03525), we reported a novel type of peroxidase mimic with record high efficiency. Our peroxidase mimic was engineered by depositing Ir atoms as ultrathin skins (a few atomic layers) on Pd nanocubes (i.e., Pd-Ir cubes). The Pd-Ir cubes exhibited significantly enhanced efficiency that is over 400-fold higher than that of natural peroxidase. In this talk, I will introduce the rational design, experimental synthesis, and mechanistic understanding of such a new peroxidase mimic. At the end, using human prostate specific antigen as a model example, I will highlight the application of our peroxidase mimic in ultrasensitive detection of disease biomarkers.