Kyle Francis Biegasiewicz
Emory University, GA·Chemistry
Adding a halogen atom, such as chlorine, bromine, iodine or fluorine, to a molecule is one of the most important reactions in making drugs. It is also used to tweak existing drugs to improve how they work.
- Fields
Chemistry
Biochemistry
- Topics
biocatalysis
enzymatic halogenation
vanadium-dependent haloperoxidase
- Grants
- 1 known grant, through Aug 2029
What they work on
- Develop new enzyme-driven oxidation and bond-forming reactions using enzymatic halide recycling, in which vanadium-dependent haloperoxidases repeatedly oxidize a small amount of halide salt with hydrogen peroxide.
- Create defunctionalative halogenation reactions that use VHPO enzymes to replace an existing functional group on a molecule with a halogen atom.
- Develop VHPO-catalyzed halooxidation reactions that add both a halogen and an oxygen atom, and apply these methods to make compounds relevant to drug discovery.
More about the research
But common halogenation methods use reagents that react with air or moisture and often put halogens in the wrong places, creating unwanted byproducts. Enzymes, nature's catalysts, are highly selective and more sustainable. This project develops halogenating enzymes as tools for chemical synthesis.
Why it matters
Pharmaceutical chemists rely on halogenation but struggle with unselective, sensitive reagents and waste byproducts. Selective VHPO enzyme reactions that use simple salts and hydrogen peroxide could offer a cleaner, more precise way to make drug intermediates and biologically active compounds.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Sebastien Laulhe
Indiana University-Purdue University-Indianapolis, IN·Chemistry
Design aryl radicals with tuned steric bulk and electronic properties, generated from light-activated electron-donor-acceptor (EDA) complexes, to remove hydrogen atoms selectively from specific C(sp3)-H bonds.
Xiongyi Huang
Johns Hopkins University, MD·Chemistry
Engineer metalloenzymes — proteins with a catalytic metal center — to perform C–H functionalization reactions absent from natural biology, installing chemical groups of biomedical relevance into organic substrates.
Vladimir Gevorgyan
University of Texas at Dallas, TX·Chemistry
Develop a visible light–induced hybrid method that combines a transition-metal catalyst with radical steps to convert unactivated C(sp3)–H bonds, the single carbon–hydrogen bonds common in drugs, without acids or added oxidants.
The school
Emory University: 70 labs on PI Pages, $1.2B a year on research, 286 research doctorates a year.
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