Emily Dykhuizen
Purdue University, IN·Biochemistry
DNA in a cell is not naked: it is wound around proteins into chromatin, and chemical tags on those proteins decide which genes stay switched off. When that packaging goes wrong, cancers can grow and can stop responding to chemotherapy.
- Fields
Biochemistry
Chemistry
Pharmacology
- Topics
chromatin
chromodomain
Polycomb Repressive Complex 1
- Grants
- 1 known grant, through Mar 2030
What they work on
- Develop CBX8 chromodomain inhibitors with improved cell permeability by selecting focused DNA-encoded libraries — small-molecule collections barcoded with DNA — designed for cellular activity rather than binding affinity alone.
- Resynthesize hit molecules off their DNA barcodes and measure affinity and selectivity against a panel of CBX chromodomains in vitro, to confirm they discriminate CBX8 from the CBX2, 4, 6 and 7 paralogs.
- Test whether cellularly active inhibitors engage CBX8 inside cells and disrupt Polycomb Repressive Complex 1-mediated chromatin compaction and gene silencing.
- Evaluate in vivo whether selective CBX8 inhibition is an effective and non-toxic therapeutic strategy, building on evidence that the CBX8 chromodomain is a target in MLL-AF9 leukemia.
More about the research
One tag, trimethylation of histone 3 at lysine 27 (H3K27me3), is altered in many cancers but is also needed for normal cells, so blocking it wholesale is a blunt instrument. Work here takes a sharper approach: target the specific protein module that reads that tag in the cancers where it matters.
Why it matters
Polycomb complexes help drive tumor growth and chemotherapy resistance, but broadly disrupting them harms normal cells. Inhibitors that hit one CBX protein at a time would be research tools for separating each paralog's role in cancer and could point toward less toxic treatments, with MLL-AF9 leukemia as the first test case.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Chongwoo Kim
Midwestern University-Glendale, AZ·Biochemistry
Systematically characterize secondary protein-protein interactions that act as selective checkpoints in assembling distinct PRC1 complexes, using X-ray crystallography, analytical ultracentrifugation and biolayer interferometry.
Nicholas Woods
University of Nebraska Medical Center, NE·Medicine & Clinical Research
Test whether Tazemetostat, which blocks the gene-silencing complex PRC2, prevents chemotherapy-induced shifts in tumor subtype, using organoids grown from tumors of Black and White PDAC patients.
G Greg Wang
Duke University, NC·Biochemistry
Characterize how the previously unstudied intrinsically disordered region of the RNA-binding protein MSI2 drives liquid-liquid phase separation, using purified proteins in vitro and in living cells.
The school
Purdue University: 43 labs on PI Pages, $932M a year on research, 833 research doctorates a year.
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