Andrew McShan, Ph.D.

Andrew McShan, Ph.D.

Andrew McShan

Assistant Professor

The questions that keep us up at night are: How does the immune system present and recognize antigens to combat disease? What are the molecular features involved in stimulating robust and specific immune responses? How can we exploit distinct features of immune recognition to develop new treatments for disease? Our research centers on answering these important questions. We focus on the CD1 family of major histocompatibility complex class I (MHC-I) related proteins, which present both self and foreign lipids to αβ, γδ, and natural killer T cells. Examples of CD1 complexes involved in the adaptive and innate immune response to human disease include those associated with lipids derived from cancerous cells (Leukemia, Carcinoma, Lymphoma, Melanoma), wasp/bee venom including yellowjackets of the genus Vespula who represent Georgia Tech's mascot Buzz (Hymenoptera venom allergy), bacterial pathogens (Mycobacterium tuberculosis - Tuberculosis, Borrelia burgdorferi - Lyme Disease, Pseudomonas aeruginosa - Pneumonia), viral pathogens (HSV-1 - Herpes, HBV - Hepatitis B), marine sponges, and self cells in autoimmune disease (Dermatitis, Psoriasis, Lysosomal Storage Disease). Recent studies have shown that CD1 can also associate with and present a much broader range of antigens, such as skin oils that lack a discernible hydrophilic head group, lipopeptides, and non-lipid small molecules. Unlike peptide antigen presentation by high polymorphic human MHC-I complexes for which therapeutics must be tailored to a patients genetic background, the non-polymorphic nature of CD1 means that lipid/CD1 molecules are attractive candidates for donor-unrestricted (i.e. universal and patient-haplotype independent) vaccines and immunotherapy treatments. Progress in the development of lipid/CD1 mediated therapies has been hindered by an incomplete understanding in several important features of the CD1 antigen processing and presentation pathway as well as a lack of structural information for clinically relevant lipid/CD1 complexes. We aim to address these knowledge gaps with our research.
 

andrew.mcshan@chemistry.gatech.edu

404.385.6052

Office Location:
MoSE G022

Website

Research Focus Areas:
  • Chemical Biology

IRI Connections:

Facundo Fernandez

Facundo Fernandez

Facundo Fernandez

Vasser Woolley Foundation Chair in Bioanalytical Chemistry
Professor; School of Chemistry and Biochemistry

Facundo was born in Buenos Aires, Argentina. He received his MSc in Chemistry from the College of Exact and Natural Sciences, Buenos Aires University in 1995 and his PhD in Analytical Chemistry from the same University, in 1999.  In August 2000, he joined the research group of Prof. Richard N. Zare in the Department of Chemistry at Stanford University.  His work focused on several aspects of Hadamard transform time-of-flight mass spectrometry with an emphasis on coupling this technique to capillary-format separation methods.  In 2002, he joined the group of Prof. Vicki Wysocki in the Department of Chemistry at the University of Arizona, to develop novel tandem mass spectrometers for gas-phase peptide ion studies. In 2004 he joined the School of Chemistry and Biochemistry at the Georgia Institute of Technology where he currently holds the position of Vasser-Woolley Endowed Professor in Bioanalytical Chemistry and Associate Chair for Research and Graduate Training. He is the author of over 185 peer-reviewed publications and numerous invited presentations at national and international conferences. He has received several awards, including the NSF CAREER award, the CETL/BP Teaching award, the Ron A. Hites best paper award from the American Society for Mass Spectrometry, and the Beynon award from Rapid Communications in Mass Spectrometry, among others. He serves on the editorial board of The Analyst and as an Associate editor for the Journal of the American Society for Mass Spectrometry. His current research interests include the field of metabolomics and the development of new ionization, imaging, machine learning and ion mobility spectrometry tools for probing composition and structure in complex molecular mixtures. In his (limited) free time, Facundo enjoys a number of activities that include camping with his family, rock climbing, paddling, archery, photography and ham radio. 

facundo.fernandez@chemistry.gatech.edu

404.385.4432

Office Location:
ES&T L1244

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    Research Focus Areas:
    • Cancer Biology
    • Molecular Evolution
    • Systems Biology
    Additional Research:
    Mass Spectrometry (MS) is one of the key analytical methods used to identify and characterize small quantities of biological molecules embedded in complex matrices. Although MS has found widespread use, improvements are still needed to extend its application to the grand challenges of this century. Since starting my position at Georgia Tech in 2004, my group members and I have used an integrated strategy with roots in bioanalytical chemistry, instrumentation development, bioinformatics, and theoretical modeling to focus on questions of great societal and scientific significance. To this purpose, we have integrated with cross-cutting teams devoted to problems that range from explaining the origins of life on Earth and diagnosing cancer at an early stage, to tracking the sources and prevalence of counterfeit pharmaceuticals worldwide. The common theme along these questions is the need for highly accurate tools for quantifying, identifying, and imaging trace chemicals in complex mixtures. Research in our lab uses state-of-the-art mass spectrometry, ion mobility gas-phase separations,ultrahigh performance liquid chromatography, and new soft ion generation techniques. We investigate the obtained data using machine learning and other powerful bioinformatic approaches. Our group is very dynamic, and each student pursues more than one project at a time, usually in collaboration with other group members or with other research groups at GT or elsewhere. Graduate and undergraduate students are trained in a variety of bioanalytical instrumentation/methodologies, with an emphasis on the fundamentals. We are analytical mass spectrometrists at heart, and strive to answer "big" scientific questions or questions with a large societal impact.

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    Nicholas V. Hud

    Nicholas V. Hud

    Nicholas Hud

    Associate Director, Parker H. Petit Institute for Bioengineering and Bioscience
    Regents’ Professor of Chemistry & Biochemistry
    Director, NSF Center for Chemical Evolution

    Nicholas Hud was born and raised in Los Angeles, California. He received his B.S. degree in physics from Loyola Marymount University. His Ph.D. was conferred by the University of California, Davis for physical investigations of DNA condensation by protamine. From 1992-1995 he was a postdoctoral fellow in the biology and biotechnology research program at Lawrence Livermore National Laboratory with Rod Balhorn. From 1995-1998 he was an NIH postdoctoral fellow in the Molecular Biology Institute at UCLA where he worked with Juli Feigon and Frank A. L. Anet on the application of NMR spectroscopy to the study of DNA-cation interactions. Hud joined the faculty at Georgia Tech as an assistant professor in 1999 and was promoted to full professor in 2008. He has been visiting professor of chemistry at the National NMR Center in Slovenia, and at Imperial College London. Hud currently serves as PI of the NSF Center for Chemical Evolution, as chair of the biochemistry division of the School of Chemistry and Biochemistry, as co-director of the Georgia Tech-Emory University Center for Fundamental and Applied Molecular Evolution (FAME), and as associate director of the Petit Institute for Bioengineering and Bioscience.

    nick.hud@chemistry.gatech.edu

    404-385-1162

    Office Location:
    Petit Biotechnology Building, Office 1108

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    Research Focus Areas:
    • Drug Design, Development and Delivery
    • Molecular Evolution
    Additional Research:
    Intercalation-mediated Nucleic Acid Assembly, The Molecular Midwife & the Origin of Life, Nucleic Acid-Cation Interactions, Understanding DNA & RNA Condensation. The research in our laboratory is directed towards elucidating the fundamental chemical and physical principles that govern nucleic acid (RNA and DNA) assembly. We are interested in how the physical properties of nucleic acids govern biological functions in contemporary life, and how these same properties provide clues to the origin and early evolution of life. We are also applying our knowledge of nucleic acids to problems that are of current importance in medicine and biotechnology. Specific projects include investigations of: 1) the origin and evolution of RNA; 2) cation, solvent and small molecule interactions with nucleic acids; 3) nucleic acid condensation and packaging; and 4) folding and evolution of the ribosome. Our research involves the application of a wide variety of physical and chemical techniques.

    IRI Connections:

    Loren Williams

    Loren Williams

    Loren Williams

    Professor
    Director, Center for the Origin of Life
    • Loren Williams is from Seattle. He received his B.Sc. in Chemistry from the University of Washington, where he worked in the laboratory of Martin Gouterman. He received his Ph.D. in Physical Chemistry from Duke University, where he worked the laboratory of Barbara Shaw. He was an American Cancer Society Postdoctoral Fellow at Harvard, and an NIH Postdoctoral Fellow at MIT with Alexander Rich. He is currently a Professor in the School of Chemistry and Biochemistry at Georgia Tech. Loren is a Fellow of the AAAS and of the International Society for the Study of the Origins of Life. He was previously Director of the NASA Astrobiology Institute funded RiboEvo Center and is currently Director of the NASA-funded Center for the Origins of Life (COOL). Loren is currently a Co-Lead of the Prebiotic Chemistry and Early Earth Environment Consortium (PCE3 a NASA Research Coordination Network). Loren has received the following awards: 
    • 1995 NSF Career Award 
    • 1996 Sigma Xi Best Paper from Georgia Tech 
    • 2012 Georgia Tech Student Advisement Award 
    • 2012 Petit Institute Above and Beyond Award 
    • 2013 Georgia Tech Faculty Award for Academic Outreach 
    • 2013 Georgia Tech College of Science Faculty Mentor Award 
    • 2017 Access Alley Award from Georgia Tech Disability Services for advocating for handicapped students 
    • 2019 Vasser Woolley Award for Excellence in Instruction 
    • 2020-21 Georgia Tech Outstanding Achievement in Research Program Development 
    • 2021 Fellow of the International Society for Study of the Origin of Life 
    • 2021 Petit Institute Above and Beyond Award 
    • 2022 College of Sciences, Faculty Mentor Award 
    • 2023 Fellow of the AAAS

    loren.williams@chemistry.gatech.edu

    404-385-6258

    Office Location:
    Petit Biotechnology Building, Office 1309

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    Research Focus Areas:
    • Molecular Evolution
    Additional Research:
    We study folding and structure of RNA and DNA as modulated by sequence, covalent damage, anti-cancer drugs, proteins, other nucleic acid molecules. The oldest assembly in biology is the ribosome, which is a primary focus of our efforts. Ancient ribosomal structure and function, from beyond the root of the tree of life, can be inferred from extant structure/function combined with phylogeny, evolutionary theory, biophysical chemistry, bioinformatics and molecular biology. We use all of these approaches to construct models of ancient ribosomes, which we then study by biochemical methods. Three-dimensional structure, being more conserved over evolutionary time than sequence, offers some of the most important guideposts in our journeys down the base of the tree of life.

    IRI Connections:

    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

    IRI Connections:

    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
    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.

    IRI Connections:

    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
    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.

    IRI Connections:

    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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