Raquel Lieberman

Raquel Lieberman
raquel.lieberman@chemistry.gatech.edu
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Raquel Lieberman is the Sepcic-Pfeil Professor of Chemistry & Biochemistry at Georgia Tech. Her research program focuses on biophysical and structural characterization of proteins and the impact of disease-associated mutations on function or dysfunction (e.g. aggregation). Rooted in basic research, the long-term goal of her research program is to convert mechanistic discoveries into disease-modifying therapies.

A major research project in her lab is investigations of glaucoma-associated herocilin, which has been funded by NIH since March 2011. Her lab has made major strides toward detailed molecular understanding of herocilin structure, function, and disease pathogenesis. They have divulged similarities between herocilin-associated glaucoma and other protein misfolding disorders, particularly aherloid diseases. Cumulatively, their work is leading to the first disease-modifying glaucoma therapeutic.

Lieberman also has a track record in membrane enzymes dating back to her thesis work where she solved the first crystal structure of the copper-dependent particulate methane monooxygenase. During her postdoc she shifted focus to intramembrane aspartyl proteases (IAPs), particularly those involved in neurodegenerative disease like Alzheimer’s disease. In her independent lab she developed new proteomics-based assays to measure IAP proteolysis. The lab also collaborates with physicists at Oak Ridge National Labs to use neutron scattering to probe structure and lipids in solution. This work has been funded by NSF and NIH.

She serves on the Executive Council of the Protein Society and as an academic editor for PLoS Biology. She also serves as co-PI of the Department of Education GAANN program in Biochemistry & Biophysics at Georgia Tech and on the advisory committees in a variety of capacities.

Professor
Phone
404-385-3663
Office
Petit Biotechnology Building, Office 1308
Additional Research
The Lieberman research group focuses on biophysical and structural characterization of proteins involved in misfolding disorders. One major research project in the lab has been investigations of the glaucoma-associated myocilin protein. The lab has made major strides toward detailed molecular understanding of myocilin structure, function, and disease pathogenesis. Our research has clearly demonstrated similarities between myocilin glaucoma and other protein misfolding disorders, particularly amyloid diseases. The work has led to new efforts aimed at amelioratingthe misfolding phenotype using chemical biology approaches. Our second project involves the study of membrane-spanning proteolytic enzymes, which have been implicated disorders such as Alzheimer disease. Our group is tackling questions surrounding discrimination among and presentation of transmembrane substrates as well as the enzymatic details of peptide hydrolysis. In addition to the biochemical characterization of intramembrane aspartyl proteases, our group is developing new crystallographic tools to improve the likelihood of determining structures of similarly challenging membrane proteins more generally.
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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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Francisco Robles

Francisco Robles
francisco.robles@bme.gatech.edu
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Dr. Francisco Robles is currently an adjunct assistant professor in the School of ECE and an assistant professor in the Wallace H. Coulter Department of Biomedical Engineering at the Georgia Institute of Technology and Emory University. He runs the Optical Imaging and Spectroscopy (OIS) Lab which focuses on advancing optical technologies to help improve the understanding of biological processes and the ability to identify and stage disease. The team develops and applies novel label-free linear and nonlinear spectroscopic methods, along with advanced signal processing methods, to gain access to novel forms of functional and molecular contrast for a variety of applications, including cancer detection, tumor margin assessment, and hematology. 

Dr. Robles completed a Postdoctoral Fellowship in the Department of Chemistry at Duke University (2016), earned his Ph.D. in Medical Physics at Duke University (2011), and earned a B.S. in Physics and in Nuclear Engineering from North Carolina State University (2007).

Associate Professor
Phone
404-385-2989
Office
UAW 3110
Research Focus Areas
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Steve Stice

Steve Stice
sstice@uga.edu
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Steve Stice is Co-Founder and Chief Scientific Officer of ArunA Biomedical, Inc, where he directs the company’s clinical and research operations. He is also University of Georgia, DW Brooks Distinguished Professor and Director of the Regenerative Bioscience Center, and holds a Georgia Research Alliance Eminent Scholar endowed chair. 

Prior to joining ArunA, Stice was the co-founder and served as both Chief Scientific Officer and Chief Executive Officer of Advanced Cell Technology, the first U.S. company to advance to human clinical trials using human pluripotent stem cells. He also co-founded startups Prolinia and Cytogenesis, the latter of which has since merged with ViaCyte. 

Stice was recruited to the University of Georgia by the Georgia Research Alliance (GRA) and holds an endowed chair as a GRA Eminant Scholar. Additionally, Stice serves as the Director of the Univeristy of Georgia’s Regenerative Bioscience Center, co-directs The Regenerative Engineering and Medicine Research Center (REM), a joint collaboration between Emory University, Georgia Institute of Technology and UGA, is a group leader of Emergent Behaviors of Integrated Cellular Systems, a National Science Foundation Center founded by the Massachusetts Institute of Technology. Stice also sits on the toxicology Scientific Advisory Board for the Food and Drug Administration (FDA). 

Stice received a Masters of Science in Reproductive Biology from Iowa State University and a Doctor of Philosophy, Developmental Biology and Embryology, from the University of Massachusetts.

D.W. Brooks Distinguished Professor
Co-Director, Regenerative Engineering and Medical Center (REM)
Director, UGA Regenerative Bioscience Center
Georgia Research Alliance Eminent Scholar
Phone
706-583-0071
Additional Research
Finding new treatments for degenerative diseases such Parkinson's, Alzheimer's and Multiple Sclerosis andneural injuries spinal cord and head trauma as well as treating cardiovascular diseases (heart and blood vessel repair) through stem cell technologies. Animal stem cells and cloning animal agriculture, veterinary and biomedicine applications.
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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.
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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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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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Roman Mezencev

Roman Mezencev
roman.mezencev@biosci.gatech.edu
https://orcid.org/0000-0003-4361-7628

Roman Mezencev is an adjunct associate professor in the School of Biological Sciences at Georgia Tech and a scientist at the U.S. EPA’s National Center of Public Health and Environmental Assessment. His areas of research interest include cancer biology, pharmacology, toxicogenomics, protein misfolding diseases, and public health. In cancer biology, his main research focuses on using omics data to identify new cancer subtypes through molecular profiling, which can help enhance their diagnosis and treatment. Additionally, Mezencev explores the use of omics data to predict and understand chemically-induced cancer and other adverse outcomes to protect public health. He is also investigating the intriguing epidemiological associations and mechanistic connections between cancer and Alzheimer’s disease (AD), as well as other protein-misfolding diseases. By understanding these associations, we can identify shared risk factors and molecular mechanisms that can lead to the development of new anti-cancer and anti-AD drugs and enhance our understanding of these complex diseases.
 

Adjunct Associate Professor, School of Biological Sciences
Phone
404-992-0151
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Mark Styczynski

Mark Styczynski
mark.styczynski@chbe.gatech.edu
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Mark Styczynski is an Associate Professor in the School of Chemical & Biomolecular Engineering at the Georgia Institute of Technology (Georgia Tech), doing research at the interface of synthetic and systems biology as applied to metabolic systems. His synthetic biology work focuses on the development of low-cost, minimal-equipment biosensors for the diagnosis of nutritional deficiencies in the developing world. His systems biology work uses computational and experimental methods to characterize metabolic dynamics and regulation using metabolomics data. He has received young investigator awards from the NSF, DARPA, and ORAU. He has won multiple department-and institute-level teaching awards at Georgia Tech. He founded and was the first president of the Metabolomics Association of North America (MANA), and is a Council Member in the Engineering BiologyResearch Consortium.

Professor
Phone
404-894-2825
Office
EBB 4013
Additional Research
Modelling and controlling metabolic dynamics and regulation (metabolic engineering). Biofuels. Systems biology-based experimental and bioinformatics analysis of metabolism Synthetic biology for the development of biosensors and diagnostics The main focus of theStyczynski groupis the experimental and computational study of the dynamics and regulation of metabolism, with ultIMaTe applications in metabolic engineering, biotechnology, and biosensors/diagnostics.
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Pamela Peralta-Yahya

Pamela Peralta-Yahya
pperalta-yahya@chemistry.gatech.edu
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Peralta-Yahya has been part of Georgia Tech since 2012. Her diverse research group composed of chemists, biologists, and chemical engineers works in the area of engineering biology, drawing from principles of biochemistry and engineering to build systems for chemical detection and production. Specifically, her group focuses on the development of G protein-coupled receptors for biotechnology and biomedical applications, and the engineering of biological systems for the production of fuels and functionalized plant natural products. Early on, her work was recognized with several awards including a DARPA Young Faculty Award, a DuPont Young Professor Award, a Kavli Fellowship by the US Academy of Science, and an NIH MIRA award. Her group’s key accomplishments are 1) the standardization of GPCR-based sensors in yeast to reduce the cost and accelerate the pace of drug discovery for these receptors, which are the target of over 30% of FDA approved drugs, and 2) the development of advanced biofuels, including pinene, which, when dimerized, has sufficient energy content to power rockets and missiles.  Today, her group is funded to work on these and other cutting edge areas – including how to power a rocket returning from Mars and how to make synthetic cells learn without evolution – by the National Institutes of Health, the National Science Foundation, the Department of Energy, and NASA.

Associate Professor, School of Chemistry and Biochemistry
Phone
404.894.4228
Office
MoSE 2100P
Additional Research

Bio-Inspired Materials; Biofuels; Cell biophysics; Cellular Materials; Biochemistry; Biomanufacturing; Energy; Biomaterials

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