Abstract
Proteomic analysis offers great diagnostic relevance, because unlike DNA, different cells in an organism express different proteins. In fact, the cellular proteome can vary as a function of time or in response to stimuli. Beyond amino acid sequence, protein function depends on chemical modifications known as post-translational modifications (PTMs) that serve as “switches” and “signals” that activate or inhibit vital functions. Despite advances in mass spectrometry, which have led to the development of fully automated protein sequencing instruments, the mapping of PTMs remains a challenge. The interaction of intense near-infrared femtosecond laser pulses with isolated molecules or ions leads to the creation of radical-ion species through an ultrafast process known as tunnel ionization. The resulting unstable ions fragment according to predictable dissociation pathways. Progress analyzing and controlling the fundamental processes taking place during photoionization and fragmentation of small polyatomic molecules has led to the development of femtosecond laser-induced ionization/dissociation (fs-LID) for proteomic analysis. Fs-LID has been proven effective for the mapping of phosphorylation sites as well as other PTMs along the peptide backbone. The fundamental steps involved in fs-LID, which permits cleavage of strong bonds while leaving chemically labile bonds intact, are discussed. Numerous examples are given to illustrate this exciting new ion activation method, and potential applications are identified.
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Acknowledgements
The instrument used for the fs-LID work was funded by grant 156 of the 21st Century Jobs Trust Fund of the SEIC Board from the State of Michigan. Additional support comes from grant CRIF ID 0923957 from the National Science Foundation. The results presented here would not be available without the work of very talented colleagues. We specifically thank Professors Gavin E. Reid and A. Daniel Jones who collaborated in the initial development of the fs-LID method. We are also thankful for the careful and persistent work on the effects of pulse shaping on molecular fragmentation by Xin Zhu, and the analysis and suggestion of multiple experiments by Dr. Vadim V. Lozovoy,
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Dantus, M., Kalcic, C.L. (2014). Ultrafast Ionization and Fragmentation: From Small Molecules to Proteomic Analysis. In: de Nalda, R., Bañares, L. (eds) Ultrafast Phenomena in Molecular Sciences. Springer Series in Chemical Physics, vol 107. Springer, Cham. https://doi.org/10.1007/978-3-319-02051-8_8
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DOI: https://doi.org/10.1007/978-3-319-02051-8_8
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