Category: Seminars

Seminar

Steven M. Firestine

Our Fall Seminar Series starts today! We welcome Dr. Steven Firestine from Wayne State University. The virtual seminar will begin at 3 p.m. today (Sept. 18) via Zoom.

Adventures in Antimicrobial Drug Discovery: Purine Biosynthesis and Spore Germination

Abstract: Antibiotics are arguably one of the greatest achievements in medical science, yet their utility is slowly being eroded by the rise of antibiotic-resistant bacteria. To combat this problem, new antibiotics focused on novel targets are desperately needed. Unfortunately, the pharmaceutical industry has divested from antimicrobial drug discovery leaving only small biotechnology companies and academia to find the next generation of antibiotics. One approach is to focus on underexplored pathways that are different between microbes and humans. Previous research has shown that the de novo purine biosynthetic pathway is different in bacteria, yeast and fungi than it is in humans. The difference is centered on the synthesis of the intermediate carboxyaminoimidazole ribonucleotide (CAIR). CAIR is synthesized from aminoimidazole ribonucleotide (AIR) and in microbes, two enzymes are required. In contrast, humans need only one enzyme. Genetic studies have shown that deleting the genes necessary for CAIR synthesis in microbes renders them avirulent. The Firestine laboratory has been focused on the interesting biochemical differences in the enzymes responsible for CAIR synthesis as well as exploiting this dissimilarity in drug discovery. The laboratory has also been exploring agents to prevent the germination of C. difficile spores. C. difficile is a challenging infection that is commonly found in hospitals and nursing homes. Spore germination is regulated by bile salts and we have discovered potent bile salt analogs which prevent germination in the nanomolar range even while in the presence of millimolar concentrations of the germinate. This seminar will outline our research on these projects.

Bio: Steve was born in Kalamazoo, MI, and attended the University of Michigan where he majored in chemistry.  While at UM, Steve conducted undergraduate research in the laboratory of Dr. James Coward working on the synthesis of fluorinated leucovorin. Steve graduated UM with high honors in chemistry and joined the Department of Medicinal Chemistry and Pharmacognosy at Purdue University where he studied medicinal chemistry and biochemistry under the direction of Dr. V. Jo Davisson. His doctoral studies focused on the study of AIR carboxylase and his research showed that this enzyme was different in microbes versus humans. Steve synthesized numerous nucleoside and nucleotide analogs including NAIR, which is the most potent inhibitor of AIR carboxylase known to date. Steve graduate in 1996 and conducted a Damon Runyon Walter Winchell Postdoctoral Fellowship in the laboratory of Dr. Stephen J. Benkovic at the Pennsylvania State University.  Steve conduct research into protein engineering and the generation of artificial transcriptional switches.  In 2000, Steve began his independent academic career as an assistant professor of medicinal chemistry at Duquesne University in Pittsburgh, PA.  There, his research focused on DNA bending agents as a mechanism to control gene expression. In 2005, Steve moved to Wayne State University and he was promoted to full professor in 2016. Since his arrival at WSU, Steve has been continuously funded by the National Institutes of Health where his research has focused on antimicrobial drug discovery.     


2018 UP ACS Student Research Symposium

Symposium logo, Upper Peninsula of Michigan with a research logoThe Upper Peninsula ACS Student Research Symposium will be held Saturday, April 14th at Northern Michigan University in Marquette, Michigan. The purpose of the symposium is to provide a venue for students to present their research in chemistry, chemical engineering, and related fields. This symposium will be an excellent opportunity for students, faculty, and the community at large to learn about the interesting research being conducted in the UP! The event is sponsored by the Upper Peninsula Section of the American Chemical Society.

Undergraduate and Graduate students, pursuing research projects through externally-funded grants, guided independent study, or as part of a course are encouraged to present at the symposium. No Cost to Present! For more information on how to present or travel support please see event details.


Sarah Green to Present at Michigan Tech Research Forum

It is a privilege and honor to announce Sarah Green (Chem/GLRC) was selected from nominees across campus as the Spring 2018 Distinguished Lecturer.

Green was nominated by Mike Abbott, director of the Great Lakes Research Center Operations, and was selected from a highly competitive pool of candidates from all colleges and schools on campus.

Her lecture, “Expanding Spheres: Atoms to Earth, Local to Global, Science to Society,” will be presented at 4 p.m. Feb. 15, in MUB Ballroom A, in a format encouraging networking and discussions.

“Sarah has been part of several major climate-related/environmental monitoring efforts over the last 15 years, beginning with KITES, the very successful 2002 NSF-funded project that spawned nearly every other subsequent environmental monitoring effort in the upper great lakes. This work continues today with the Army Corps of Engineers, the Alliance for Coastal Technologies and NOAA/GLOS. Long a favorite lecturer on campus, Sarah Green, a 2013-2014 Jefferson Science Fellow with the U.S. State Department, relates to her audience in a concise and engaging manner.”

—Mike Abbott, director of the Great Lakes Research Center Operations

The Distinguished Lecture Series began in Fall 2016 to honor faculty for their research impact both in the peer-reviewed scientific realm, but also having a direct connection to society. Department chairs, center/institute directors, deans and Research Advisory Council members nominate highly engaging presenters with broad topic appeal.

Distinguished Lecturers are selected for their ability to increase the knowledge breadth of our community by connecting their research with societal and community concerns. Topics are broad intentionally, spanning all colleges and schools at Michigan Tech.

Nominees are reviewed by a committee and announced at the beginning of fall and spring semesters. Past Distinguished Lecturers include Richelle Winkler (SS) in Fall 2016, Simon Carn (GMES) in Spring 2017, and John Vucetich (SFRES) in Fall 2017.

For more information and to nominate yourself or others, visit the Michigan Tech Research Forum.

by Adrienne Minerick, Assistant to the Provost for Faculty Development


Climate Discussion Tonight

During the Nov. 3, 2016, Climate Café event, Robert Handler of Michigan Tech’s Sustainable Futures Institute discusses energy efficiency and ways to mitigate climate change. (Video by Keweenaw Now)

The fourth in a series of discussions on climate change will take place from 6 to 8 p.m. tonight at the Orpheum/Studio Pizza in Hancock.

The purpose of this fourth event in the series is to continue the discussions about what activities and topics we should focus on as a local community when we think about climate change impacts and our responses to those impacts.

There are lots of potential strategies to mitigate or adapt to the impacts of climate change, and we want to gather a community of interested people who will help plan the future priorities for our grassroots organization. We will have a few five minute presentations from local people who are developing responses to climate change, and then we will break into groups according  to your interests, and start making plans.

The series is organized by the Keweenaw Climate Community, sponsored by the local chapter of the American Chemical Society and the Department of Social Sciences at Michigan Tech.

More can be found out by reading this story in Keweenaw Now.


Communicating Climate Science: Consensus Matters

Dr. Sarah Green, Professor
Department of Chemistry
Michigan Technological University
Date: April 22, 2016
Place: Chem-Sci Room 101
Time: 3:00 pm

Abstract

Climate science does not translate directly into political action to curb climate change. We are conducting a global experiment by modifying the basic chemistry, physics, and biology of the planet. Climate science explains past changes and projects the possible outcomes of this experiment according to parameters that are adjusted through political decisions. The public cannot be expected to grasp all the details of climate science. Yet public acceptance of its key findings is essential to support climate policy. Recognition of the consensus among experts is a gateway to accepting the reality of climate change. How do we know there is a scientific consensus and how do we communicate that fact to the public?


At the End of Chemistry

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.


Atomistic Resolution Dances of Membrane Proteins by NMR

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/


Engineering Bimetallic Nanostructures as Peroxidase Mimics for Disease Diagnosis

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.


ON THE PROTECTIVE PROPERTIES OF GLYCINE BASED OSMOLYTES IN A THIOL REDUCING ENVIRONMENT

Michigan Technological University
Department of Chemistry
John Hausman
Advisor: Dr. Ashutosh Tiwari
Master’s Defense
Monday August 10, 2015
9:30 am, Chem-Sci 101

ON THE PROTECTIVE PROPERTIES OF GLYCINE BASED OSMOLYTES IN A THIOL REDUCING ENVIRONMENT

The protective properties of osmolytes have been studied intently for decades. Originally used to aid in the crystallization of proteins in x-ray diffraction studies, these cosolvents have been shown to reverse protein denaturation and aggregation. Osmolytes aid extremophiles in surviving harsh environments by preferentially excluding themselves from the surface of the protein, thus directing water molecules to the protein’s surface. Their use is increasing and affects the everyday consumer as these osmolytes are naturally found in many health foods and also in many daily use products such as shampoo. Consumers also supplement their diets with thiol-based antioxidants such as glutathione as part of healthier life style. However, thiol-based antioxidants in high concentration have been known to cause un-intended health issues that relate to its disulfide reducing property. The disulfide-reducing agent can cleave the proteins’ disulfide-bonds and promote misfolding and aggregation. In this thesis, we investigated the influence of commonly consumed glycine-based osmolytes on providing stability to proteins against a disulfide-reducing agent. We chose glycine, sarcosine (N-methyl glycine), di-methyl glycine (DMG), and betaine (N,N,N-trimethylglycine) with increasing number of methyl groups. An added benefit to studying this class of osmolytes is to also investigate the impact N-methyl substitution has on the osmolytes’ protective properties. We studied the effect of these osmolytes on protein aggregation using spectroscopic techniques such as UV-visible absorbance, intrinsic fluorescence and extrinsic fluorescence measurements. In addition, we carried out non-reducing SDS-PAGE to check for higher order aggregates and characterized morphology of these aggregates using scanning electron microscopy. Overall, our results show that of all the osmolytes used, glycine was the best stabilizer followed by sarcosine. Betaine and dimethylglycine did not provide effective protection against disulfide-reducing influence.