Raman spectroscopy has historically damaged live proteins during optical measurements, leading to inconsistent results. Researchers from Texas A&M University and TEES have introduced a new approach called thermostable-Raman-interaction-profiling (TRIP), allowing low-concentration, low-dose screenings for protein-to-ligand interactions in relevant conditions, promising label-free, highly reproducible measurements, and potential applications in rapid and cost-effective drug, vaccine, and virus testing, and DNA analysis.
Raman spectroscopy, a technique for analyzing chemicals by projecting monochromatic light onto a sample and observing the scattered light that comes out, has been a source of frustration for biomedical researchers for over 50 years. The heat produced by the light almost destroys live proteins during the optical measurements, resulting in reduced and non-repeatable results. As of recently, however, those frustrations may now be a thing of the past.
A group of researchers with the Institute for Quantum Sciences and Engineering at Texas A&M University and the Texas A&M Engineering Experiment Station (TEES) have developed a new technique that allows low-concentration and low-dose screenings of protein-to-ligand interactions in physiologically relevant conditions. Titled thermostable-Raman-interaction-profiling (TRIP), this new approach is a paradigm-shifting answer to a long-standing problem that provides label-free, highly reproducible Raman spectroscopy measurements.
“Protein is a very fragile biological molecule and needs specific care,” said lead author and postdoctoral research assistant Dr. Narangerel Altangerel. “When I cool down the surface or substrate, I can make the proteins happy. I can poke them with the laser, and they can now output the information I need.”
While the proteins studied are on a molecular level, the implications of these findings could be huge. Like a lock and key, a protein-ligand interaction is the first step in processes like signal transduction, immune responses, and gene regulation. Due to TRIP’s ability to detect protein-ligand interactions in real-time, the timeline for drug and vaccine testing may be shortened. Another application could be clinical, turning lengthy tests to detect a DOI: 10.1073/pnas.2218826120
The project is supported by the Air Force Office of Scientific Research (AFOSR), the Office of Naval Research, the Robert A. Welch Foundation, TEES, the
