Eranthie Weerapana
Boston College, MA·Chemistry
Among the twenty amino acids that build proteins, cysteine is unusually reactive. That reactivity lets individual cysteines do specialized jobs: speeding up chemical reactions, sensing oxidation, or gripping metal atoms.
- Fields
Chemistry
Biochemistry
Pharmacology
- Topics
chemoproteomics
cysteine
covalent ligands
- Grants
- 1 known grant, through Mar 2031
What they work on
- Dissect how iron-sulfur clusters, metal cofactors essential for energy metabolism, are assembled on mitochondrial proteins by profiling the cysteines involved with compartment-targeted chemoproteomic probes.
- Measure cysteine oxidation on proteins near the plasma membrane during growth-factor signaling, using proximity biotinylation enzymes such as TurboID or APEX to restrict labeling to that region of the cell.
- Build electrophilic phage display libraries of cyclic peptides carrying reactive groups to find covalent ligands for proteins on the outer surface of cells.
- Map which cysteines on nuclear proteins can be bound by small molecules and prioritize the binding events that change how those proteins associate with chromatin, the protein-DNA complex that packages the genome.
More about the research
It also makes cysteine the favorite handle for covalent drugs, which latch onto a protein permanently. The challenge is finding which cysteines in a cell actually matter. This research program builds chemical probes and chemoproteomic methods — strategies that tag reactive cysteines across thousands of proteins at once and read them out by mass spectrometry — to map functional cysteines and to create small molecules that bind them and change what the protein does.
Why it matters
Cysteine chemistry sits behind several disease processes named in this work: iron-sulfur cluster defects in Friedreich's ataxia, redox and chromatin regulation in cancer, and clotting biology relevant to thrombosis. Mapping which cysteines are reactive, oxidation-sensitive or bindable in a given compartment could reveal new therapeutic targets and supply the covalent ligands needed to test them, including peptide-based ligands for proteins on the cell surface that conventional drugs struggle to reach.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Peijian He
Georgia State University, GA·Medicine & Clinical Research
Test whether losing frataxin, a mitochondrial iron-handling protein, causes ferroptosis (iron-driven cell death) and liver injury in MASLD mouse models, and whether restoring frataxin prevents this damage.
Jaewon Chang
Emory University, GA·Chemistry
Design and synthesize covalent warheads that react with lysine, tyrosine and serine residues on E3 ubiquitin ligases, the enzymes that tag proteins for destruction, going beyond the cysteine-reactive chemistry used so far.
Seiya Kitamura
Albert Einstein College of Medicine, NY·Chemistry
Couple the SuFEx click-chemistry high-throughput medicinal chemistry platform with covalent ligands, molecules that bond permanently to proteins, to develop chemical probes for individual underexplored proteins that lack distinct binding sites.
The school
Boston College: 11 labs on PI Pages, $96M a year on research, 161 research doctorates a year.
Reach out
A start for your email. Fill in the brackets.