Recent breakthroughs at the Institute for Quantum Sciences and Engineering at Texas A&M University as well as the Texas A&M Engineering Experiment Station (TEES) have solved a decade-long issue with protein analysis using Raman spectroscopy. The researchers developed a new technique called thermostable-Raman-interaction profiling (TRIP) that allows researchers to analyze protein-ligand interaction in a highly reproducible way.
Due to the heat generated by Raman spectroscopy nearly destroying live proteins, reproducible analysis is challenging using traditional methods. Using the new TRIP technique, which is published in Proceedings of the National Academy of Sciences, it becomes possible to analyze protein-ligand interactions in a highly accurate and reproducible way. This real-time analysis of these interactions will lead to shorter testing times for drugs and vaccines, as well as having clinical applications by reducing virus detection times. The technique also allows researchers to use smaller or less concentrated samples, making the technique highly cost-effective.
“The whole idea from the spectroscopy statute is that it requires minimum to none for sample preparation, so this can be moved into the clinic right away,” said Dr. Vladislav Yakovlev, Texas A&M Professor in the Department of Biomedical Engineering. “Clinicians and patients don’t have to wait for days and weeks of analysis. You can get all these answers almost right away.”
The researchers intend to continue studying other potential applications of the technique in the biological sciences. “In a follow-up article, we are trying to identify the chemical composition of those proteins just using this technique so we can apply this to similar ideas related to DNA analysis and other biological molecules,” Yakovlev said. “Something that normally requires sequencing but utilizes TRIP, so you don't need any sample preparation.”