Benjamin Partridge
University of Rochester, NY·Chemistry
Proteins and nucleic acids (DNA and RNA) only work when they fold into the right shapes and assemble in the right way. They are mostly held in those shapes by weak, reversible attractions called noncovalent interactions.
- Fields
Chemistry
Biochemistry
Biophysics
- Topics
supramolecular chemistry
noncovalent interactions
molecular recognition
- Grants
- 1 known grant, through Jun 2029
What they work on
- Establish structure-function relationships for amphiphilic molecules that assemble into supramolecular capsules, linking molecular design to assembly and to how well they block amyloid beta fragments from forming fibers.
- Build light-responsive photoswitches into supramolecular chaperones so their water-avoiding character can be changed on demand inside the sample, to push misfolded proteins to refold.
- Develop bifacial nucleobases, building blocks that base-pair on two faces, that recognize standard Watson-Crick-Franklin and non-standard or mismatched base pairs in specific DNA and RNA sequences and folds.
- Target nucleic acid structures that lack clear binding pockets by using natural base-pairing rather than small-molecule intercalators, which slide between bases.
More about the research
Most drugs and diagnostic agents are small molecules with fixed structures. These molecules are often much smaller than the structures they try to control, and they cannot change shape over time. This research program proposes a different strategy. It aims to build synthetic assemblies, held together by the same kind of weak interactions, that match the size and flexibility of their biological targets. This field is called supramolecular chemistry. The work has two directions: artificial helpers for protein folding, and new ways to recognize specific DNA and RNA structures.
Why it matters
Protein clumping and unusual DNA or RNA structures play roles in disease. For example, amyloid beta aggregation is linked to Alzheimer's disease, and mismatched DNA bases are linked to DNA damage. Synthetic chaperones that block aggregation could help with protein misfolding problems. Bifacial nucleobases that recognize specific genetic structures could lay groundwork for future diagnostics and therapies. Mainly, the work adds basic understanding of how molecules recognize biomolecular structures.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Dennis Bong
Ohio State University, OH·Chemistry
Synthesize bifacial peptide nucleic acid probes that bind U-rich internal loops in folded RNA by forming base triples, and test how broadly this loop motif works as a general targeting handle in structured RNAs.
James MacKay
Elizabethtown College, PA·Chemistry
Design and synthesize new PNA nucleobases that improve pi-pi stacking of the peptide nucleic acid strand within PNA-double-stranded RNA triple helices, strengthening binding.
Wenqi Liu
University of South Florida, FL·Chemistry·Early-career
Design and synthesize acyclic (open-chain) receptors that use ion-dipole and electrostatic interactions to bind lithium ions selectively over competing metal ions, and measure their binding in solution.
The school
University of Rochester: 38 labs on PI Pages, $492M a year on research, 308 research doctorates a year.
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