Aditi Das

Aditi Das

Aditi Das

Associate Professor

Aditi Das did her BSc. (Hons.) Chemistry from St. Stephen's College Delhi, followed by M.S. (Chemistry) from I.I.T (Kanpur). She received her Ph.D. in Chemistry from Princeton University. She did post-doctoral work with Prof. Steve Sligar. She joined University of Illinois, Urbana-Champaign (UIUC) as a tenure track assistant professor in 2012. In 2019, she was promoted to associate professor with tenure. In 2022, she joined School of Chemistry and Biochemistry at Georgia Institute of Technology as an associate professor with tenure. Her research is in the area of enzymology of oxygenases that are involved lipid metabolism and cannabinoid metabolism.

Das is recipient of an American Heart Associate (AHA) career award and has been funded by National Institute of Health (NIH - NIGMS, NIDA and NCCIH), USDA, and National Multiple Sclerosis Society (NMSS). Her research was recognized by several National awards: Young Investigator award From Eicosanoid Research Foundation, Mary Swartz Rose Young Investigator Award and E.L.R. Stokstad award from American Society for Nutrition (ASN) for outstanding research on bioactive compounds for human health. She is also the recipient of Zoetis Research Excellence Award from her college. She was a co-organizer of the International Conference on Cytochrome P450. Recently her laboratory contributed several papers on cannabinoid metabolism by p450s. In recognition of this work, she was awarded El Sohly award from the ACS-Cannabis division for excellence in Cannabis research and is invited to give plenary lecture at ISSX meeting.  Das is also a standing study section member of BBM NIH study section. 

aditi.das@chemistry.gatech.edu

609-203-6924

Office Location:
3306 IBB

Chemistry Profile

Research Focus Areas:
  • Biobased Materials
  • Biochemicals
  • Bioengineering
  • Biotechnology
  • Cancer Immunotherapy
  • Cell Manufacturing
  • Chemical Biology
  • Drug Design, Development and Delivery
  • Health & Life Sciences
  • Neuroscience
  • Shaping the Human-Technology Frontier
  • Systems Biology

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    Raquel Lieberman

    Raquel Lieberman

    Raquel Lieberman

    Professor

    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.

    raquel.lieberman@chemistry.gatech.edu

    404-385-3663

    Office Location:
    Petit Biotechnology Building, Office 1308

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    Research Focus Areas:
  • Chemical Biology
  • Drug Design, Development and Delivery
  • Molecular, Cellular and Tissue Biomechanics
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    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

    Marcus Cicerone

    Professor

    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.

    cicerone@gatech.edu

    404-894-2761

    Office Location:
    G026 MoSE

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    Research Focus Areas:
  • Cell Manufacturing
  • Chemical Biology
  • Drug Design, Development and Delivery
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    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

    Christoph Fahrni

    Professor
    Associate Chair for Graduate and Postdoctoral Programs

    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.

    fahrni@chemistry.gatech.edu

    404-385-1164

    Office Location:
    Petit Biotechnology Building, Office 3310

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    Research Focus Areas:
  • Chemical Biology
  • Systems Biology
  • 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.

    IRI Connections:

    Ronghu Wu

    Ronghu Wu

    Ronghu Wu

    Associate Professor

    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.

    ronghu.wu@chemistry.gatech.edu

    404-385-1515

    Office Location:
    EBB 4011

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    Research Focus Areas:
  • Cancer Biology
  • Chemical Biology
  • Systems Biology

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    Adegboyega “Yomi” Oyelere

    Adegboyega “Yomi” Oyelere

    Adegboyega “Yomi” Oyelere Oyelere

    Associate Professor

    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.

    adegboyega.oyelere@chemistry.gatech.edu

    404-894-4047

    Office Location:
    Petit Biotechnology Building, Office 3305

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    Research Focus Areas:
  • Cancer Biology
  • Drug Design, Development and Delivery
  • Molecular Evolution
  • 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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    Vinayak Agarwal

    Vinayak Agarwal

    Vinayak Agarwal

    Assistant Professor

    Vinny is an Assistant Professor at Georgia Tech with joint appointments at the School of Chemistry and Biochemistry and School of Biological Sciences.

    A majority of antibiotics and drugs that we use in the clinic are derived or inspired from small organic molecules called Natural Products that are produced by living organisms such as bacteria and plants. Natural Products are at the forefront of fighting the global epidemic of antibiotic resistant pathogens, and keeping the inventory of clinically applicable pharmaceuticals stocked up. Some Natural Products are also potent human toxins and pollutants, and we need to understand how these toxins are produced to minimize our and the environmental exposure to them.

    We as biochemists ask some simple questions- how and why are Natural Products produced in Nature, what we can learn from Natural Product biosynthetic processes, and how we can exploit Nature's synthetic capabilities for interesting applications?

    Broadly, we are interested in questions involving (meta)genomics, biochemistry, structural and mechanistic enzymology, mass spectrometry, analytical chemistry, and how natural product chemistry dictates biology.

    vagarwal@gatech.edu

    404-385-3798

    Office Location:
    Petit Biotechnology Building, Office 3315

    Website

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  • Research Focus Areas:
  • Molecular, Cellular and Tissue Biomechanics
  • Additional Research:
    A majority of antibiotics and drugs that we use in the clinic are derived or inspired from small organic molecules called Natural Products that are produced by living organisms such as bacteria and plants. Natural Products are at the forefront of fighting the global epidemic of antibiotic resistant pathogens, and keeping the inventory of clinically applicable pharmaceuticals stocked up. Some Natural Products are also potent human toxins and pollutants, and we need to understand how these toxins are produced to minimize our and the environmental exposure to them. We as biochemists ask some simple questions- how and why are Natural Products produced in Nature, what we can learn from Natural Product biosynthetic processes, and how we can exploit Nature's synthetic capabilities for interesting applications? Broadly, we are interested in questions involving (meta)genomics, biochemistry, structural and mechanistic enzymology, mass spectrometry, analytical chemistry, and how natural product chemistry dictates biology.

    IRI Connections:

    Amit Reddi

    Amit Reddi

    Amit Reddi

    Associate Professor

    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.      

    amit.reddi@chemistry.gatech.edu

    404-385-1428

    Office Location:
    Petit Biotechnology Building, Office 3313

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    Research Focus Areas:
  • Cancer Biology
  • Chemical Biology
  • Systems Biology
  • 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.

    IRI Connections:

    Neha Garg

    Neha Garg

    Neha Garg

    Associate Professor

    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.

    neha.garg@chemistry.gatech.edu

    404-385-5677

    Office Location:
    EBB 4016

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    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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    M.G. Finn

    M.G. Finn

    M.G. Finn

    Chair and Professor
    James A. Carlos Family Chair for Pediatric Technology

    We develop chemical and biological tools for research in a wide range of fields. Some of them are briefly described below; please see our group web page for more details. Chemistry, biology, immunology, and evolution with viruses. The sizes and properties of virus particles put them at the interface between the worlds of chemistry and biology. We use techniques from both fields to tailor these particles for applications to cell targeting, diagnostics, vaccine development, catalysis, and materials self-assembly. This work involves combinations of small-molecule and polymer synthesis, bioconjugation, molecular biology, protein design, protein evolution, bioanalytical chemistry, enzymology, physiology, and immunology. It is an exciting training ground for modern molecular scientists and engineers. Development of reactions for organic synthesis, chemical biology, and materials science. Molecular function is what matters most to our scientific lives, and good chemical reactions provide the means to achieve such function. We continue our efforts to develop and optimize reactions that meet the click chemistry standard for power and generality. Our current focus is on highly reliable reversible reactions, which open up new possibilities for polymer synthesis and modification, as well as for the controlled delivery of therapeutic and diagnostic agents to biological targets. Traditional and combinatorial synthesis of biologically active compounds.We have a longstanding interest in the development of biologically active small molecules. We work closely with industrial and academic collaborators on such targets as antiviral agents, compounds to combat tobacco addiction, and treatments for inflammatory disease.

    Faces of Research - Profile Article

    mgfinn@gatech.edu

    404-385-0906

    Office Location:
    MoSE 2201B

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    Research Focus Areas:
  • Biomaterials
  • Drug Design, Development and Delivery
  • Molecular Evolution

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