Multiplatform High-Definition Ion Mobility Separations of the Largest Epimeric Peptides
Thurman, Hayden A. Wijegunawardena, Gayani Berthias, Francis Williamson, David L. Wu, Haifan Nagy, Gabe Jensen, Ole N. Shvartsburg, Alexandre A.
Thurman, Hayden A.
Wijegunawardena, Gayani
Berthias, Francis
Williamson, David L.
Wu, Haifan
Nagy, Gabe
Jensen, Ole N.
Shvartsburg, Alexandre A.
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2024-02
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Article
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Ion mobility spectrometers,Isomers,Mass spectrometry
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Citation
Thurman, H.A., Wijegunawardena, G., Berthias, F., Williamson, D.L., Wu, H., Nagy, G., Jensen, O.N., & Shvartsburg, A.A. (2024). "Multiplatform High-Definition Ion Mobility Separations of the Largest Epimeric Peptides." Analytical Chemistry. https://doi.org/10.1021/acs.analchem.3c03079.
Abstract
Ion mobility spectrometry (IMS) coupled to mass spectrometry (MS) has become a versatile tool to fractionate complex mixtures, distinguish structural isomers, and elucidate molecular geometries. Along with the whole MS field, IMS/MS advances to ever larger species. A topical proteomic problem is the discovery and characterization of d-amino acid-containing peptides (DAACPs) that are critical to neurotransmission and toxicology. Both linear IMS and FAIMS previously disentangled D/L epimers with up to ~30 residues. In the first study using all three most powerful IMS methodologies--trapped IMS, cyclic IMS, and FAIMS--we demonstrate baseline resolution of the largest known D/L peptides (CHH from $Homarus americanus$ with 72 residues) with a dynamic range up to 100. This expands FAIMS analyses of isomeric modified peptides, especially using hydrogen-rich buffers, to the ~50-100 residue range of small proteins. The spectra for D and L are unprecedentedly strikingly similar except for a uniform shift of the separation parameter, indicating the conserved epimer-specific structural elements across multiple charge states and conformers. As the interepimer resolution tracks the average for smaller DAACPs, the IMS approaches could help search for yet larger DAACPs. The a priori method to calibrate cyclic (including multipass) IMS developed here may be broadly useful.
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American Chemical Society
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Analytical Chemistry
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0003-2700