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Michael C. Fitzgerald

Professor of Chemistry
Chemistry
Box 90346, Durham, NC 27708-0346
3222 French Science Center, 124 Science Drive, Durham, NC 27708

Overview


Dr. Fitzgerald’s research group is focused on studies of protein folding and function. The group utilizes a combination of covalent labeling strategies (e.g. protein amide H/D exchange and methionine oxidiation) and mass spectrometry techniques to investigate the thermodynamic properties of protein folding and ligand binding reactions. Current research efforts involve: (1) the development new biophysical methods that enable protein folding and stability measurements to be performed on the proteomic scale; and (2) the application of these new methods in the areas of disease detection, diagnosis, and therapy.

Current Appointments & Affiliations


Professor of Chemistry · 2011 - Present Chemistry, Trinity College of Arts & Sciences
Chair of Chemistry · 2024 - Present Chemistry, Trinity College of Arts & Sciences
Professor of Biochemistry · 2011 - Present Biochemistry, Basic Science Departments

In the News


Published October 19, 2016
Dust Mite Allergens Share Rare Combo of Qualities

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Recent Publications


Discovery of Host-Directed Small Molecules with Broad Anti-Leishmanial Efficacy.

Journal Article bioRxiv · November 4, 2025 Leishmaniasis, a neglected tropical disease affecting nearly 10% of the global population, suffers from limited therapeutic options and rising drug resistance. To address this, we developed 343 analogs of AR-12, a compound that has previously illustrated h ... Full text Link to item Cite

Leveraging Vulnerabilities in Copper Trafficking for Synergistic Antifungal Activity.

Journal Article ACS chemical biology · November 2025 Candida albicans is an opportunistic fungal pathogen that causes millions of infections per year, for which more efficacious treatments are needed. Observations that azole antifungals incite C. albicans to adjust a variety of metal-dependent ... Full text Cite

Copper Activates a Redox Switch to Reversibly Inhibit Glyceraldehyde-3-Phosphate Dehydrogenase.

Journal Article Biochemistry · November 2025 Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), one of the most conserved proteins across all kingdoms of life, has a multitude of moonlighting functions beyond its enzymatic role in glycolysis. Metal binding to GAPDH has previously been reported to inhi ... Full text Cite
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Recent Grants


Pharmacological Sciences Training Program

Inst. Training Prgm or CMEPreceptor · Awarded by National Institutes of Health · 2025 - 2030

Chemical Biology Strategies to Resolve Plasmodium Heat Shock Protein Function

ResearchCo Investigator · Awarded by National Institute of Allergy and Infectious Diseases · 2023 - 2028

Noncovalent interaction of mutant KRAS inhibitors

ResearchCo Investigator · Awarded by National Cancer Institute · 2025 - 2027

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Education, Training & Certifications


University of Wisconsin, Madison · 1994 Ph.D.
Davidson College · 1989 B.S.