In general, mass spectrometry is one of the most important “eyes” of the pharmaceutical industry. Basically, it could be compared to a super-sensitive pair of scales that not only tells us how heavy a molecule is, but also helps to identify it. Furthermore, it even reveals if a drug or medicine has been contaminated. Thus, researchers can verify that they have managed to produce the molecule they originally planned or intended to.
- Analytical chemistry is the field of science that aims to identify certain components and determine their quantity and quality. Some of these may not have been known to us before. Large molecules, such as proteins, have a lot of variants that are only slightly different from one another. One of the major challenges that the pharmaceutical industry routinely faces is how to filter out and control these variants. This is where mass spectrometry comes into the picture- said Attila Gáspár, professor of analytical chemistry at the Faculty of Science and Technology of the University of Debrecen.
Professor Gáspár explained that, during mass spectrometry measurements, salts and other small molecules in the sample often tend to either suppress the signal from proteins or contaminate the instrument. Therefore, a time-consuming purification or chromatographic separation of the sample is required. A research group at the Department of Inorganic and Analytical Chemistry at UD’s Faculty of Engineering and Technology has found a new, simple, yet rather effective solution that allows them to “see” the protein without having to implement purification. The gist of their method lies in the dynamics of the flow in the capillary.
- In a way different from usual practice, we injected a small portion of the sample to be examined into the mass spectrometer through a long and thin capillary tube, when we noticed that the protein signal was much stronger and clearer at the very beginning of the sample than in the middle. This contradicted our previous experience, according to which proteins would often stick to the wall and we would expect them to appear at the end of the sample. Then, a theoretical expert at a conference pointed out that this could be a phenomenon of Taylor-Aris dispersion- said Attila Gáspár.
- Due to this dispersion phenomenon, proteins with low diffusion rates form a much more spread-out zone than small molecules, which is why some of the proteins leave the matrix materials behind at the end of the capillary. The protein thus reaches the detector before the interfering substances, giving us a clear picture without any need for time-consuming purification or chromatographic separation- summarized the professor.
Measurements can be taken directly from the original sample by using this method, which drastically speeds up the process of analysis and provides researchers with accurate results even from much smaller samples than before, which significantly reduces the cost of testing, too. This can result in huge savings for a pharmaceutical company, where hundreds or thousands of samples are measured day by day.
The article about this scientific discovery, for which Attila Gáspár received the Count István Tisza Foundation for the University of Debrecen Publication Award, was published in Angewandte Chemie, one of the most prestigious international journals on chemistry.
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