Evolution of Mass Spectrometry Methods in Biology Over the Last Three Decades
- mshafaei87
- Apr 3, 2024
- 3 min read
Written by: M.Amin Shafaei, SMA
Date: Apr 3, 2024
Abstract
Over the last 30 years, mass spectrometry has undergone significant evolution, markedly enhancing biological research. This article offers a detailed exploration of the methods used in mass spectrometry within the biological sciences, providing a comparative analysis of their developments and applications. Focusing on methodologies developed after the year 2000, we underscore the pivotal transitions that have shaped the current state of mass spectrometric analysis in biology.
Introduction
Mass spectrometry (MS) has proven to be an indispensable analytical tool in biology, contributing profoundly to the understanding of complex biological processes and systems. The turn of the millennium marked the beginning of rapid advancements in MS, driven by the need for greater sensitivity, resolution, and speed in the analysis of biological samples (Aebersold & Mann, 2003).
Methods in Mass Spectrometry for Biological Analysis
Electrospray Ionization (ESI) and Matrix-Assisted Laser Desorption/Ionization (MALDI) have been the two dominant ionization techniques in biological MS since their inception. ESI-MS became a method of choice for the analysis of proteins and peptides in solution, favored for its ability to analyze biomolecules in their native state (Fenn et al., 1989). MALDI-MS, in contrast, became widespread for its rapid analysis of proteins from solid samples (Karas & Hillenkamp, 1988).
Tandem MS, or MS/MS, has enabled detailed structural elucidation of biomolecules. This method involves the isolation of a particular ion of interest followed by its fragmentation to produce a set of daughter ions, which are then analyzed to infer the structure of the parent molecule (Wells & McLuckey, 2005).
Recent Advances in MS
In the past two decades, the development of Orbitrap and quadrupole time-of-flight (Q-TOF) mass analyzers has significantly improved the resolution and accuracy of mass spectrometric measurements. Orbitrap analyzers, in particular, offer high-resolution mass measurements, which are crucial for the identification and quantification of proteomes (Hu et al., 2005).
Ion mobility spectrometry-mass spectrometry (IMS-MS) has emerged as a method that adds an additional dimension of separation based on the shape and charge of ions, thus enhancing the analysis of complex biological samples (Shvartsburg & Smith, 2008).
Comparative Analysis
Each of these methods has its advantages and limitations. ESI is highly compatible with liquid chromatography, making it ideal for online separations, while MALDI's high-throughput capability makes it suitable for rapid screening applications. MS/MS provides detailed structural information but can be limited by the complexity of the sample. Orbitrap analyzers offer high resolution and mass accuracy but may require more maintenance and expertise. IMS-MS provides additional separation capabilities, which can be advantageous for isomeric compounds but may add complexity to the overall analysis.
Conclusion
The advancements in mass spectrometry over the past three decades have been pivotal in advancing biological research. From ESI and MALDI to the development of Orbitrap and IMS-MS, each method has contributed uniquely to the field. The choice of method often depends on the specific requirements of the biological question being addressed, such as the need for structural information, sensitivity, or throughput.
References
Aebersold, R., & Mann, M. (2003). Mass spectrometry-based proteomics. Nature, 422(6928), 198-207.
Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., & Whitehouse, C. M. (1989). Electrospray ionization for mass spectrometry of large biomolecules. Science, 246(4926), 64-71.
Hu, Q., Noll, R. J., Li, H., Makarov, A., Hardman, M., & Cooks, R. G. (2005). The Orbitrap: a new mass spectrometer. Journal of Mass Spectrometry, 40(4), 430-443.
Karas, M., & Hillenkamp, F. (1988). Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Analytical Chemistry, 60(20), 2299-2301.
Shvartsburg, A. A., & Smith, R. D. (2008). Fundamentals of traveling wave ion mobility spectrometry. Analytical Chemistry, 80(24), 9689-9699.
Wells, J. M., & McLuckey, S. A. (2005). Collision-induced dissociation (CID) of peptides and proteins. Methods in Enzymology, 402, 148-185.
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