A Breakthrough in Spectroscopy Overcomes Five Decades of Challenges
For years, Raman spectroscopy has adversely affected live proteins during optical analysis, yielding unreliable outcomes. However, a novel technique known as Thermostable-Raman-Interaction-Profiling (TRIP), pioneered by researchers from Texas A&M University and the Texas A&M Engineering Experiment Station (TEES), has now emerged. This method enables screenings at low concentrations and doses for interactions between proteins and ligands under conditions that are physiologically relevant. The technique offers the advantage of label-free and highly consistent readings, with promising applications in the quick and cost-efficient testing of drugs, vaccines, viruses, and DNA.
For over half a century, biomedical scientists have faced difficulties with Raman spectroscopy. This analytic method involves shining a single-wavelength light onto a sample and then studying the light that is scattered as a result. The heat generated by the light has been detrimental to live proteins involved in the measurement process, leading to inconsistent and irreproducible findings. This obstacle now appears to be surmountable.
Developed by the Institute for Quantum Sciences and Engineering at Texas A&M University in collaboration with TEES, the TRIP methodology represents a transformative solution to a problem that has persisted for decades. It allows for highly reliable Raman spectroscopy assessments without requiring labels.
Dr. Narangerel Altangerel, the study’s lead author and a postdoctoral research assistant, noted the delicate nature of proteins. “Upon cooling the surface or substrate, it becomes possible to interact with the proteins using a laser, enabling them to release the necessary information,” he said.
The consequences of this advancement are far-reaching. Protein-ligand interactions serve as the initial steps in numerous biological processes such as signal transduction, immune reactions, and gene control. TRIP’s capacity to detect these interactions in real time could significantly accelerate the timelines for testing drugs and vaccines. In a clinical setting, the technique could transform protracted viral detection tests into same-day procedures with precise results.
Dr. Vladislav Yakovlev, a co-author and University Professor in the Department of Biomedical Engineering, emphasized the immediacy of its clinical application. “Given that minimal to no sample preparation is needed, this method can be directly introduced into clinical practice,” he stated.
Moreover, TRIP’s reduced requirements for sample size and protein concentration make it a more cost-effective option for analysis.
“While I previously had to share an expensive sample among multiple people, resulting in a small sample size that made Raman analysis difficult, this innovation challenged me to explore new avenues,” added Altangerel.
While the discovery is groundbreaking, the research team is also exploring additional applications for the TRIP method.
“In subsequent research, we aim to identify the chemical composition of proteins using this technique, thereby extending its applicability to DNA analysis and other biological molecules,” said Yakovlev.
The research project has received funding from various institutions including the Air Force Office of Scientific Research (AFOSR), the Office of Naval Research, the Robert A. Welch Foundation, TEES, the National Institutes of Health, and the Texas A&M University X Grants Program. The collaborative effort involved multiple departments and was supported by a team consisting of both faculty and students from the Institute for Quantum Sciences and Engineering. Other contributing authors include Dr. Benjamin Neuman, Dr. Philip Hemmer, Navid Rajil, Dr. Zhenhuan Yi, Dr. Alexei Sokolov, and principal investigator Dr. Marlan Scully. Dr. Sofi Bin-Salamon served as the program officer for the AFOSR.
Frequently Asked Questions (FAQs) about Raman spectroscopy breakthrough
What is the new breakthrough in Raman spectroscopy?
The new breakthrough is a technique known as Thermostable-Raman-Interaction-Profiling (TRIP), developed by researchers from Texas A&M University and the Texas A&M Engineering Experiment Station (TEES). TRIP allows for low-concentration and low-dose screenings of interactions between proteins and ligands under physiologically relevant conditions. It offers label-free and highly consistent Raman spectroscopy measurements.
What problem does the TRIP technique solve?
The TRIP technique addresses the longstanding issue of damaging live proteins during Raman spectroscopic analysis, which has led to inconsistent and unreliable results. TRIP enables more accurate and reproducible measurements without adversely affecting the proteins involved.
Who are the primary researchers behind this development?
The primary researchers are affiliated with the Institute for Quantum Sciences and Engineering at Texas A&M University and TEES. The lead author of the study is Dr. Narangerel Altangerel, a postdoctoral research assistant.
How could this breakthrough impact drug and vaccine testing?
TRIP has the potential to significantly accelerate the timelines for drug and vaccine testing. Its ability to detect protein-ligand interactions in real time and under physiologically relevant conditions could make the testing processes faster and more efficient.
What are the potential clinical applications of the TRIP technique?
The TRIP technique could be applied in clinical settings for rapid virus detection tests, yielding same-day, precise results. Its minimal to non-existent requirements for sample preparation make it a readily deployable method in clinical environments.
Is the TRIP technique cost-effective?
Yes, the TRIP technique requires smaller sample sizes and lower protein concentrations, which makes it a more cost-effective method for conducting tests.
Who funded the research for this breakthrough?
The research was funded by various institutions including the Air Force Office of Scientific Research (AFOSR), the Office of Naval Research, the Robert A. Welch Foundation, TEES, the National Institutes of Health, and the Texas A&M University X Grants Program.
Are there plans for future research?
Yes, the research team is exploring additional applications of the TRIP method, including its potential use in identifying the chemical composition of proteins and in DNA analysis.
Who else contributed to this research?
The research involved a multidisciplinary team including Dr. Benjamin Neuman from the Department of Biology, Dr. Philip Hemmer from the Department of Electric and Computer Engineering, and several other researchers from the Institute for Quantum Sciences and Engineering at Texas A&M University. Dr. Sofi Bin-Salamon served as the program officer for the AFOSR.
More about Raman spectroscopy breakthrough
- Proceedings of the National Academy of Sciences
- Texas A&M University Institute for Quantum Sciences and Engineering
- Texas A&M Engineering Experiment Station (TEES)
- Air Force Office of Scientific Research (AFOSR)
- Office of Naval Research
- Robert A. Welch Foundation
- National Institutes of Health
- Texas A&M University X Grants Program