Faculty Profiles

Katherine J. Franz
Katherine J. Franz
Professor in the Department of Chemistry
Office: 
2103 French Science Center, 124 Science Drive, Durham, NC 27708
Phone: 
(919) 660-1541
katherine.franz@duke.edu
Franz Research Group
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.

Overview

Education:

Ph.D., Massachusetts Institute of Technology 2000

B.A., Wellesley College 1995

Research Areas:
Biomolecular Structure and Function, Inorganic

Hašková, Pavlína, et al. “Cardioprotective effects of iron chelator HAPI and ROS-activated boronate prochelator BHAPI against catecholamine-induced oxidative cellular injury.” Toxicology, vol. 371, Sept. 2016, pp. 17–28. Epmc, doi:10.1016/j.tox.2016.10.004. Full Text

Jansová, Hana, et al. “Characterization of cytoprotective and toxic properties of iron chelator SIH, prochelator BSIH and their degradation products.” Toxicology, vol. 350–352, Mar. 2016, pp. 15–24. Epmc, doi:10.1016/j.tox.2016.03.004. Full Text

Franks, Andrew T., et al. “A multifunctional, light-activated prochelator inhibits UVA-induced oxidative stress.” Bioorganic & Medicinal Chemistry Letters, vol. 25, no. 21, Nov. 2015, pp. 4843–47. Epmc, doi:10.1016/j.bmcl.2015.06.048. Full Text

Pushie, M. Jake, et al. “Model Peptide Studies Reveal a Mixed Histidine-Methionine Cu(I) Binding Site at the N-Terminus of Human Copper Transporter 1.” Inorganic Chemistry, vol. 54, no. 17, Sept. 2015, pp. 8544–51. Epmc, doi:10.1021/acs.inorgchem.5b01162. Full Text

Alies, Bruno, et al. “A prochelator peptide designed to use heterometallic cooperativity to enhance metal ion affinity.” Chemical Science, vol. 6, no. 6, June 2015, pp. 3606–10. Epmc, doi:10.1039/c5sc00602c. Full Text

Crumbliss, Alvin L., et al. “Preface. Biometals 2014--Proceedings of the 9th International Symposium Biometals 2014 at Duke University, Durham, NC, USA.” Biometals, vol. 28, no. 3, June 2015, p. 431. Pubmed, doi:10.1007/s10534-015-9854-8. Full Text

Helsel, Marian E., and Katherine J. Franz. “Pharmacological activity of metal binding agents that alter copper bioavailability.” Dalton Transactions (Cambridge, England : 2003), vol. 44, no. 19, May 2015, pp. 8760–70. Epmc, doi:10.1039/c5dt00634a. Full Text

Bureš, Jan, et al. “LC-UV/MS methods for the analysis of prochelator-boronyl salicylaldehyde isonicotinoyl hydrazone (BSIH) and its active chelator salicylaldehyde isonicotinoyl hydrazone (SIH).” Journal of Pharmaceutical and Biomedical Analysis, vol. 105, Feb. 2015, pp. 55–63. Epmc, doi:10.1016/j.jpba.2014.11.044. Full Text

Safi, Rachid, et al. “Copper signaling axis as a target for prostate cancer therapeutics.” Cancer Res, vol. 74, no. 20, Oct. 2014, pp. 5819–31. Pubmed, doi:10.1158/0008-5472.CAN-13-3527. Full Text Open Access Copy

Franks, Andrew T., and Katherine J. Franz. “A prochelator with a modular masking group featuring hydrogen peroxide activation with concurrent fluorescent reporting.” Chemical Communications (Cambridge, England), vol. 50, no. 77, Oct. 2014, pp. 11317–20. Epmc, doi:10.1039/c4cc05076b. Full Text

Pages

Liu, L. L., and K. J. Franz. “Characterization of metal binding sites in a synthetic phosphorylated alpha-synuclein peptide fragment.” Abstracts of Papers of the American Chemical Society, vol. 229, AMER CHEMICAL SOC, 2005, pp. U1080–81.

Franz, Katherine J., et al. “Development of lanthanide-binding peptides as natively expressed protein probes.” Journal of Inorganic Biochemistry, vol. 96, no. 1, Elsevier BV, 2003, pp. 131–131. Crossref, doi:10.1016/s0162-0134(03)80614-1. Full Text

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