Philipp Schmidpeter
University of Texas at San Antonio, TX·Biophysics
TRP channels are pores in cell membranes that open in response to many kinds of signals, from temperature to chemicals inside the cell. They are found throughout the body.
- Fields
Biophysics
Biochemistry
Physiology
- Topics
TRP channels
transient receptor potential channels
ion channels
- Grants
- 1 known grant, through Aug 2030
What they work on
- Identify membrane lipids that modulate TRP ion channel activity, using cell-based experiments designed for the membrane environment.
- Identify cytosolic proteins, including protein-folding helper enzymes, that regulate TRP channels, using cell-based experiments designed for the cytosolic environment.
- Reconstitute TRP channels with these lipid and protein partners from purified components, and use biophysical, functional and structural studies to build quantitative models of channel regulation.
More about the research
Beyond their well-known roles in acute and chronic pain, they have been linked to kidney disease, neurodegeneration, diabetes and heart disorders. Much is known about their structure and about drugs that act on them. Far less is known about how the cell's normal surroundings control them.
Why it matters
TRP channels play central roles in pain, kidney disease and heart rhythm problems. A clearer picture of how lipids and helper proteins control these channels in the body could provide a framework for designing new drugs that target them in specific diseases.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
John Bankston
University of Colorado Denver/Anschutz Medical Campus, CO·Biophysics
Determine how single-tail lipids, including polyunsaturated fatty acids, lysophosphatidyl cholines and N-acyl amino acids, bind to ASIC3, an acid-sensing ion channel, and how they boost or open it.
Tom A Rapoport
Harvard University, MA·Biochemistry
Determine how misfolded glycoproteins, proteins carrying sugar chains, are delivered to the Hrd1 complex and moved from the ER interior across the membrane, building on cryo-electron microscopy structures.
Conor McClenaghan
Rutgers University-New Brunswick, NJ·Pharmacology
Develop engineered split-SUR2 subunits, protein pieces of the KATP channel's regulatory partner, that can reassemble and restore ATP-sensitive potassium channel function in vivo, using protein engineering and patch clamp recordings.
The school
University of Texas at San Antonio: 10 labs on PI Pages, $172M a year on research, 129 research doctorates a year.
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