Marcus Cicerone

Marcus Cicerone
cicerone@gatech.edu
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Marcus T Cicerone received his Ph.D. from the University of Wisconsin – Madison in 1994, under the direction of Mark Ediger. He spent three years at Johnson & Johnson Clinical Diagnostics, served as a visiting teaching professor at Brigham Young University for two years, and subsequently joined the National Institute of Standards and Technology in 2001, where he remained for 18 years, serving as a group leader and project leader. In January 2019 he joined the Georgia Institute of Technology as a Professor of Chemistry. 

Professor Cicerone is a fellow of American Physical Society, and has received several awards for his efforts in coherent Raman-based biological imaging and for his work in dynamics of liquids and amorphous solids. These include a Johnson & Johnson Director’s Research Award, two Department of Commerce Bronze metals, the 2015 Washington Academy of Sciences Physical & Biological Sciences Award, and the 2017 Arthur S. Flemming Award.

Professor
Phone
404-894-2761
Office
G026 MoSE
Additional Research
Professor Cicerone works on development and application of spectroscopic coherent Raman imaging approaches and on dynamics of amorphous condensed matter. In the coherent Raman imaging work, his group introduced broadband (spectroscopic) coherent anti-Stokes Raman scattering (BCARS) microscopy in 2004. Since then he and his group have remained at the forefront of this field, introducing improvements such as a time-domain Kramers-Kronig transform to deal with non-causal signals for retrieving the pure Raman spectrum directly from the raw BCARS signal. The results of that work and other instrument design innovations utilizing impulsive vibrational coherence generation resulted in recognition as one of the top 10 innovations in BioPhotonics for 2014. His group has logged many imaging firsts, including the first to obtain quantitative vibrational fingerprint spectra from mammalian cells using coherent Raman imaging, and the first to identify specific structural proteins from coherent Raman imaging.His work on dynamics of amorphous condensed matter focuses on the impact of picosecond timescale spatial and temporal heterogeneity in dynamics on transport and relaxation in liquids and glasses. In 2004, he used neutron scattering to show for the first time that chemical and physical stability of proteins encapsulated in glassy sugars could be predicted by the profile of ps-timescale dynamics. Since then, he has developed a framework for calculating transport and relaxation properties of liquids and glasses over 12 orders of magnitude in time, based solely on ps-timescale dynamics, and identified the molecular origin of a relaxation process (Johari-Goldstein process) that had been observed but remained enigmatic for 50 years. He has also developed benchtop approaches accessible to pharmaceutical labs for measuring the relevant dynamics, and developed a protein stability approach for drug delivery that encapsulates proteins in nanometer-sized droplets of vitrified sugar-based glass and makes them impervious to traditional processing steps, allowing retention of ~99% of protein function or titer after all processing steps. This approach has now been used successfully in large animal trials, and has also been shown to be effective for transdermal drug delivery due to the nanometer size of the encapsulation materials.
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Christoph Fahrni

Christoph Fahrni
fahrni@chemistry.gatech.edu
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Christoph Fahrni earned a master’s degree in chemistry from the Federal Institute of Technology (ETH, Switzerland) and a Ph.D. degree in chemistry from the University of Basel (Switzerland). After working as a postdoctoral fellow at Northwestern University (Evanston, IL), he joined the School of Chemistry and Biochemistry at the Georgia Institute of Technology in 1999.

Professor
Associate Chair for Graduate and Postdoctoral Programs
Phone
404-385-1164
Office
Petit Biotechnology Building, Office 3310
Additional Research
Metals In Biological Systems. Approximately one third of all known proteins contain metal ions as cofactors and serve a wide variety of functions, such as structure stabilization, catalysis, electron transfer reactions or complex tasks, including signal transduction and gene regulation. Numerous diseases such as haemochromatosis or Menkes disease were found to be related with a defect in metal metabolism. Research is concerned with development of metal specific fluorescent probes for the investigation of the intracellular chemistry of trace elements, the mechanistic study of metalloprotein catalyzed reactions with unusual coordination geometries as well as the development of protein-based, semisynthetic organometallic catalysts in aqueous solution. Fluorescence Probes and Chelators for the Investigation of Intracellular Storage, Trafficking, and Homeostasis of Trace Elements. Until recently, little was known about how eukaryotic cells take up metal ions or regulate intracellular concentrations. Fluorescent chemosensors have been proven to be powerful and nondestructive tools for the study of intracellular metal ion distributions and have provided a wealth of information, including control of muscle contraction, nerve cell communication, hormone secretion, and immune cell activation. Research is concerned with the development of highly specific fluorescent probes for the detailed mechanistic investigation of copper storage and trafficking. Distribution and changes of intracellular copper concentration can be followed in vivo using fluorescence microscopy. Various combinatorial fluorophore libraries are being synthesized, which subsequently are screened for copper binding selectivity. Bioorganometallic Catalysis with Peptide and Protein Ligands. The distribution of metal ions in sea water can be directly correlated with their abundance in biological systems. Consequently, the platinum metals palladium, rhodium, iridium and platinum are not found in any of the natural occurring metalloproteins. Nevertheless, these cations are excellent catalysts for a wide variety of organometallic reactions. Research is focused on combining the rich chemistry of platinum metals with the advantage of proteins to catalyze reactions with high regio- and stereo-selectivity. Novel bioorganometallic catalysts are being developed via redesign of structurally well characterized proteins.
Research Focus Areas
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Ronghu Wu

Ronghu Wu
ronghu.wu@chemistry.gatech.edu
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Research in the Wu lab is mainly focused on mass spectrometry (MS)-based proteomics. They are developing innovative methods to globally identify and quantify proteins and their post-translational modifications (PTMs), including glycosylation and phosphorylation, and applying them for biomedical research. Protein PTMs plays essential roles in biological systems, and aberrant protein expression and modification are directly related to various human diseases, including cystic fibrosis, cancer and infectious diseases. Novel analytical methods will profoundly advance our understanding of protein function, which will lead to the identification of proteins or modified proteins as effective drug targets and the discovery of biomarkers for early disease detection.

Associate Professor
Phone
404-385-1515
Office
EBB 4011
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Adegboyega “Yomi” Oyelere

Adegboyega “Yomi” Oyelere
adegboyega.oyelere@chemistry.gatech.edu
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Dr. Adegboyega “Yomi” Oyelere has received PhD from Brown University in 1998. Currently, he works as an associate professor in the School of Chemistry and Biochemistry at the Georgia Institute of Technology.

Associate Professor
Phone
404-894-4047
Office
Petit Biotechnology Building, Office 3305
Additional Research
Bioorganic Chemistry, Biochemistry and Drug Design, RNA-Small Molecule Interaction, Targeted Histone Deacetylase (HDAC) Inhibition, Design and Synthesis of Novel Bioconjugates for Molecular Delivery Applications
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Amit Reddi

Amit Reddi
amit.reddi@chemistry.gatech.edu

Metalloproteins constitute one of the largest classes of proteins in the proteome and are involved in virtually every metabolic and signaling pathway of consequence to human health and disease. Broadly speaking, the Reddi laboratory is interested in determining the cellular, molecular, and chemical mechanisms by which metalloproteins are activated by cells, and once activated, how they communicate with other biomolecules to promote normal metabolism and physiology, placing an emphasis on systems relevant to cancer, neurodegenerative disorders, and infectious diseases. Current projects in the lab are focused on elucidating heme trafficking pathways and the role of Cu/Zn Superoxide Dismutase (SOD1) in redox signaling. Prospective students will get broad training in disciplines that span modern biochemistry, bioinorganic chemistry, biophysics, chemical biology, molecular genetics, and cell biology.      

Associate Professor
Phone
404-385-1428
Office
Petit Biotechnology Building, Office 3313
Additional Research
Metalloproteins constitute one of the largest classes of proteins in the proteome and are involved in virtually every metabolic and signaling pathway of consequence to human health and disease. Broadly speaking, the Reddi laboratory is interested in determining the cellular, molecular, and chemical mechanisms by which metalloproteins are activated by cells, and once activated, how they communicate with other biomolecules to promote normal metabolism and physiology, placing an emphasis on systems relevant to cancer, neurodegenerative disorders, and infectious diseases. Current projects in the lab are focused on elucidating heme trafficking pathways and the role of Cu/Zn Superoxide Dismutase (SOD1) in redox signaling. Prospective students will get broad training in disciplines that span modern biochemistry, bioinorganic chemistry, biophysics, chemical biology, molecular genetics, and cell biology.
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Neha Garg

Neha Garg
neha.garg@chemistry.gatech.edu
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Professor Garg received a Bachelors in Engineering in Biotechnology from University Institute of Technology and Masters in Science from Indian Institute of Technology, Delhi. During her masters, she spent several months in Berlin, Germany while conducting research with Professor Marion Ansorge Schumacher at Technical University, Berlin as an DAAD Fellow. Garg obtained her Ph.D. in 2013 from the University of Illinois, Urbana Champaign under the direction of Professor Wilfred A. van der Donk and Professor Satish Nair. She then joined Professor Pieter C Dorrestein's research laboratory as a postdoctoral research associate at the University of California, San Diego. Garg joined the faculty at GeorgiaTech in 2017.

Associate Professor
Phone
404-385-5677
Office
EBB 4016
Additional Research
Eukaryotes, including humans, are 'petri dishes', hosting an abundant and a rich prokaryotic 'microbiome'. The Garg Lab aims to understand the molecular interactions between a eukaryotic host and its microbiome, and how these molecular interactions dictate human health and disease. Using a concoction of innovative tools including bioinformatics, clinical microbiology, mass spectrometry, DNA sequencing, and mass spectrometry-based 2D and 3D spatial imaging, we aim to delineate specific molecules that modulate the dynamics of microbial involvement in our response to genetic and environmental triggers of disease. We characterize the biosynthesis of these small molecule natural products to innovate developement of new therapeutics.
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Henry La Pierre

Henry La Pierre
la_pierre@chemistry.gatech.edu
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Professor, School of Chemistry & Biochemistry
Phone
(404) 385-3258
Additional Research

Nuclear

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Joseph Perry

Joseph Perry
joe.perry@chemistry.gatech.edu
Research Website
Professor, School of Chemistry and Biochemistry
Phone
(404) 385-6046
Additional Research

Analytical Chemistry; Characterization; Energy; Sustainability; Materials Chemistry; Molecular Biophysics; Nanoscience and Technology; Physical Chemistry; Polymer Chemistry; Spectroscopy; Surface and Interfacial Chemistry; Theory and Modeling

http://www.chemistry.gatech.edu/faculty/perry/
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