Wisconsin Alumni Research Foundation

Analytical Instrumentation, Methods & Materials
Analytical Instrumentation Methods Materials
Using Liquid Crystals to Detect Post-Translationally Modified Peptides
WARF: P04385US

Inventors: Nicholas Abbott, Brian Clare, Paul Bertics

The Wisconsin Alumni Research Foundation (WARF) is seeking commercial partners interested in developing devices and methods that use liquid crystals to detect post-translationally modified peptides.
Post-translational modification of proteins provides a significant means of regulating biological processes. In particular, phosphorylation is a key factor in many aspects of cell signaling, cell cycle regulation and response to stress. Because compounds that modulate phosphorylation and other post-translational modifications may be useful in the treatment of diseases and conditions such as cancer, immunosuppression, retinopathy, rheumatoid arthritis and neurodegeneration, various methods for detecting post-translational modifications have been developed; however, simple and rapid methods that do not require complex instrumentation, radioactive labeling or other manipulation are still needed.
The Invention
UW-Madison researchers have developed devices and methods that use liquid crystals to distinguish between post-translationally modified peptides and unmodified peptides. A sample containing a post-translationally modified peptide, an unmodified peptide, or a mixture of both is bound to a substrate surface. The surface then is contacted with a recognition agent, such as an antibody, that specifically binds to or forms a complex with the post-translationally modified protein in the sample. A liquid crystal is contacted with the surface, and its orientation is observed. Disruptions in the uniform anchoring of the liquid crystal indicate the presence of post-translationally modified protein.
  • Drug screening
  • Detecting post-translational modifications, including phosphorylation
Key Benefits
  • Provides a simple method of monitoring the phosphorylation status of proteins and peptides
  • Does not require radioactive labeling
  • Amenable to high throughput screening
  • Applicable to drug-screening and activity assays
For current licensing status, please contact Jennifer Gottwald at [javascript protected email address] or 608-960-9854