Overview
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.
Current Appointments & Affiliations
Professor of Chemistry
·
2015 - Present
Chemistry,
Trinity College of Arts & Sciences
Member of the Duke Cancer Institute
·
2003 - Present
Duke Cancer Institute,
Institutes and Centers
Recent Publications
Extrinsic and intrinsic factors affect copper-induced protein precipitation across eukaryotic and prokaryotic proteomes.
Journal Article Protein science : a publication of the Protein Society · June 2025 The susceptibility of a protein to aggregation upon exposure to copper ions (Cu) has been recognized as a contributor to Cu-induced cellular dysfunction and toxicity. Different cell types succumb to Cu to varying degrees, indicating innate differences betw ... Full text CiteAn Engineered Prodrug Selectively Suppresses β-Lactam-Resistant Bacteria in a Mixed Microbial Setting.
Journal Article ACS infectious diseases · June 2025 The rise of β-lactam resistance necessitates new strategies to combat bacterial infections. We purposefully engineered the β-lactam prodrug AcephPT to exploit β-lactamase activity to selectively suppress resistant bacteria producing extended-spectrum-β-lac ... Full text CiteIntramolecular Histidine Cross-Links Formed via Copper-Catalyzed Oxidation of Histatin Peptides.
Journal Article Journal of the American Chemical Society · April 2025 Histidine is a versatile amino acid with metal-binding, nucleophilic, and basic properties that endow many peptides and proteins with biological activity. However, histidine itself is susceptible to oxidative modifications via post-translational modificati ... Full text CiteRecent Grants
Tri-Institutional Molecular Mycology and Pathogenesis Training Program
Inst. Training Prgm or CMEMentor · Awarded by National Institutes of Health · 2024 - 2029Duke Preparing Research Scholars in Biomedical Sciences- Post-Baccalaureate Research Education Program
Inst. Training Prgm or CMEMentor · Awarded by National Institute of General Medical Sciences · 2022 - 2027What Does This Goo Do With Cu? Discovery of a Specific Copper Binding Site in Gel-Forming Mucins
ResearchPrincipal Investigator · Awarded by US-Israel Binational Science Foundation · 2022 - 2026View All Grants
Education, Training & Certifications
Massachusetts Institute of Technology ·
2000
Ph.D.
Wellesley College ·
1995
B.A.