Center for Biologically Inspired Materials and Material Systems Center for Biologically Inspired Materials and Material Systems
Pratt School of Engineering
Duke University

 HOME > pratt > CBIMMS    Search Help Login pdf version printable version 

Katherine J. Franz, Alexander F. Hehmeyer Professor of Chemistry and Professor of Center for Biologically Inspired Materials and Material Systems

Katherine J. Franz
Contact Info:
Office Location:  2103 FFSC
Office Phone:  (919) 660-1541
Email Address: send me a message
Web Page:  http://www.chem.duke.edu/labs/franz

Education:

Ph.D.Massachusetts Institute of Technology2000
B.A.Wellesley College1995
Specialties:

Inorganic
Biochemistry
Biomolecular Structure and Function
Synthesis
Research Interests:

Research in the Franz group is involved in elucidating the structural and functional consequences of metal ion coordination in biological systems. We are particularly interested in understanding the coordination chemistry utilized by biology to manage essential yet toxic species like copper and iron. Understanding these principles further guides our development of new chemical tools to manipulate biological metal ion location, speciation, and reactivity for potential therapeutic benefit. We use a combination of synthesis, spectroscopy, and biochemistry in our work. Please visit our group website to learn more about our research.

Areas of Interest:

Bioinorganic Chemistry

Keywords:

Aldehydes • alpha-Synuclein • Alzheimer Disease • Amides • Amines • Amino Acid Motifs • Amino Acid Sequence • Amino Acid Substitution • Amyloid beta-Peptides • Amyloid Precursor Protein Secretases • Animals • Antineoplastic Agents • Antioxidants • Apoptosis • Ascorbic Acid • Benzene Derivatives • Binding Sites • Biological Assay • Biological Transport • Boron Compounds • Boronic Acids • Calcium • Calorimetry • Carrier Proteins • Cation Transport Proteins • Cell Biology • Cell Death • Cell Line • Cell Line, Tumor • Cell Membrane • Cell Membrane Permeability • Cell Survival • Cells, Cultured • Chelating Agents • Chelation Therapy • Chromatography, High Pressure Liquid • Chromatography, Liquid • Circular Dichroism • Coordination Complexes • Copper • Cryptococcosis • Crystallography, X-Ray • Cysteine • Cysteinyldopa • Cytoprotection • Deoxyribose • Dopamine • Dose-Response Relationship, Drug • Epithelial Cells • Esters • Eukaryota • Ferric Compounds • Ferrous Compounds • Fibroblasts • Fluoresceins • Fluorescence Resonance Energy Transfer • Fluorescent Dyes • Fungal Proteins • Gene Expression Regulation • HeLa Cells • Histidine • HL-60 Cells • Homeostasis • Humans • Hydrazines • Hydrazones • Hydrogen Peroxide • Hydrogen-Ion Concentration • Hydrolysis • Hydroxyl Radical • Immunity, Innate • Indoles • Iron • Iron Chelating Agents • Isonicotinic Acids • Kinetics • Lewy Bodies • Ligands • Light • Macrophages • Magnetic Resonance Spectroscopy • Mass Spectrometry • MCF-7 Cells • Melanins • Membrane Potential, Mitochondrial • Metal ions • Metalloproteins • Metals • Methionine • Mice • Mice, Knockout • Microscopy, Fluorescence • Models, Biological • Models, Molecular • Molecular Conformation • Molecular Imaging • Molecular Sequence Annotation • Molecular Sequence Data • Molecular Structure • Molecular Targeted Therapy • Myocytes, Cardiac • Nerve Tissue Proteins • Neurodegenerative Diseases • Norleucine • Oligopeptides • Organometallic Compounds • Organoplatinum Compounds • Oxidation-Reduction • Oxidative Stress • Oxygen • Oxyquinoline • Paraquat • Parkinson Disease • Peptide Fragments • Peptides • Phosphopeptides • Phosphorylation • Phosphoserine • Phosphotyrosine • Photolysis • Prodrugs • Protein Binding • Pyridines • Quantum Theory • Reactive Oxygen Species • Receptors, Transferrin • Retinal Pigment Epithelium • RNA Interference • RNA, Messenger • RNA, Small Interfering • Semicarbazones • Signal Transduction • Silver • Spectrometry, Fluorescence • Spectrometry, Mass, Electrospray Ionization • Spectrophotometry, Infrared • Spectrophotometry, Ultraviolet • Spectrum Analysis • Stress, Physiological • Structure-Activity Relationship • Synucleins • Tandem Mass Spectrometry • Terbium • Thiazines • Time Factors • Tissue Distribution • Titrimetry • Ultraviolet Rays • Xenograft Model Antitumor Assays • Zinc

Current Ph.D. Students   (Former Students)

  • Zeenat Razvi  
  • Kacey C. Hall  
  • Qin Wang  
  • Qiang Su  
  • Andrew Franks  
  • Mark Sleeper  
  • David Besse  
  • Marian Helsel  
Postdocs Mentored

  • Bruno Alies (2013/01-present)  
  • Prof. Anupa Kumbhar (Visiting Scientist from Univ. of Pune, India) (2010 - 2011)  
  • Filip Kielar (2009 - 2012)  
  • David Pham (2006-2008)  
  • Yohannes Tesema (2004-2007)  
  • Jianfeng Jiang (2004-2005)  
Recent Publications   (More Publications)

  1. Wang, Q; Franz, KJ, The hydrolytic susceptibility of prochelator BSIH in aqueous solutions., Bioorganic & Medicinal Chemistry Letters (July, 2017) [doi]  [abs]
  2. Helsel, ME; White, EJ; Razvi, SZA; Alies, B; Franz, KJ, Chemical and functional properties of metal chelators that mobilize copper to elicit fungal killing of Cryptococcus neoformans., Metallomics, vol. 9 no. 1 (January, 2017), pp. 69-81 [doi]  [abs]
  3. Sansee, A; Meksawangwong, S; Chainok, K; Franz, KJ; Gál, M; Pålsson, L-O; Puniyan, W; Traiphol, R; Pal, R; Kielar, F, Novel aminoalkyl tris-cyclometalated iridium complexes as cellular stains., Dalton Transactions, vol. 45 no. 43 (November, 2016), pp. 17420-17430 [doi]  [abs]
  4. Wang, Q; Franz, KJ, Stimulus-Responsive Prochelators for Manipulating Cellular Metals., Accounts of Chemical Research, vol. 49 no. 11 (November, 2016), pp. 2468-2477 [doi]  [abs]
  5. Hašková, P; Jansová, H; Bureš, J; Macháček, M; Jirkovská, A; Franz, KJ; Kovaříková, P; Šimůnek, T, Cardioprotective effects of iron chelator HAPI and ROS-activated boronate prochelator BHAPI against catecholamine-induced oxidative cellular injury., TOXICOLOGY, vol. 371 (September, 2016), pp. 17-28 [doi]  [abs]


Duke University * Pratt * Reload * Login