Alberto Perez
University of Florida, FL·Biophysics
BET proteins help control which genes are active, and they are involved in viral infection and several cancers. Drugs that block BET proteins have been tried, but they hit all BET family members at once.
- Fields
Biophysics
Chemistry
Biochemistry
- Topics
BET proteins
bromodomain and extra-terminal
ET domain
- Grants
- 1 known grant, through Mar 2027
What they work on
- Map the binding partners of the ET domain of BET proteins: identify candidates computationally, rank the strongest with machine learning and physics-based methods, and check top leads with NMR experiments.
- Reveal how peptides bind the shape-shifting ET domain, and why binding strength differs across similar BET proteins, using adaptive sampling molecular dynamics and Markov State Models.
- Design new peptide binders to find the limits of binding strength for each binding mode, and test whether viruses use tighter-binding modes than the host's regulatory proteins.
- Identify hot-spot regions in the ET binding domain from the computational designs, as a basis for future selective therapeutic design.
More about the research
This causes toxicity, even though each family member has its own job and appears in different tissues. A region called the ET domain may offer a way to target one BET protein at a time. Molecules that bind it show promising selectivity, but little is known about what binds the ET domain or how.
Why it matters
Treatments targeting BET proteins in lung, breast and prostate cancer and in viral infection have failed because of toxicity and drug resistance. Explaining how the ET domain selects its binding partners could lay the groundwork for drugs that act on a single BET protein. Such drugs might avoid the side effects of current non-specific BET inhibitors.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Brian Kuhlman
University of North Carolina at Chapel Hill, NC·Biochemistry
Test whether a protein core mixing water-repelling and water-attracting amino acids yields a partly unfolded, water-containing cold state, using de novo designed cold unfolding proteins, biophysical measurements and molecular dynamics simulations.
Ronald Levy
Temple University, PA·Biophysics
Determine the physical basis of epistasis, where one mutation's effect depends on others, in HIV integrase and capsid under different drugs, using molecular dynamics simulations and virus data to build drug-specific fitness landscapes.
Jonah Vilseck
Indiana University-Purdue University-Indianapolis, IN·Chemistry
Use lambda dynamics free energy simulations to understand how missense mutations in a drug target cause drug resistance, and to identify drug modifications that overcome it.
The school
University of Florida: 65 labs on PI Pages, $1.3B a year on research, 795 research doctorates a year.
Reach out
A start for your email. Fill in the brackets.