Coupling 193 nm Ultraviolet Photodissociation and Ion Mobility for Sequence Characterization of Conformationally-Selected Peptides.
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| Title: | Coupling 193 nm Ultraviolet Photodissociation and Ion Mobility for Sequence Characterization of Conformationally-Selected Peptides. |
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| Authors: | Stiving, Alyssa Q.1 (AUTHOR), Harvey, Sophie R.1 (AUTHOR), Jones, Benjamin J.1 (AUTHOR), Bellina, Bruno2 (AUTHOR), Brown, Jeffery M.3 (AUTHOR), Barran, Perdita E.2 (AUTHOR), Wysocki, Vicki H.1 (AUTHOR) wysocki.11@osu.edu |
| Source: | Journal of the American Society for Mass Spectrometry. 11/4/2020, Vol. 31 Issue 11, p2313-2320. 8p. |
| Abstract: | Ultraviolet photodissociation (UVPD) has emerged as a useful technique for characterizing peptide, protein, and protein complex primary and secondary structure. 193 nm UVPD, specifically, enables extensive covalent fragmentation of the peptide backbone without the requirement of a specific side chain chromophore and with no precursor charge state dependence. We have modified a commercial quadrupole-ion mobility-time-of-flight (Q-IM-TOF) mass spectrometer to include 193 nm UVPD following ion mobility. Ion mobility (IM) is a gas-phase separation technique that enables separation of ions by their size, shape, and charge, providing an orthogonal dimension of separation to mass analysis. Following instrument modifications, we characterized the performance of, and information that could be generated from, this new setup using the model peptides substance P, melittin, and insulin chain B. These experiments show extensive fragmentation across the peptide backbone and a variety of ion types as expected from 193 nm UVPD. Additionally, y-2 ions (along with complementary a+2 and b+2 ions) N-terminal to proline were observed. Combining the IM separation and mobility gating capabilities with UVPD, we demonstrate the ability to accomplish both mass- and mobility-selection of bradykinin des-Arg9 and des-Arg1 peptides followed by complete sequence characterization by UVPD. The new capabilities of this modified instrument demonstrate the utility of combining IM with UVPD because isobaric species cannot be independently selected with a traditional quadrupole alone. [ABSTRACT FROM AUTHOR] |
| Copyright of Journal of the American Society for Mass Spectrometry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
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| Header | DbId: egs DbLabel: Engineering Source An: 146856177 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Coupling 193 nm Ultraviolet Photodissociation and Ion Mobility for Sequence Characterization of Conformationally-Selected Peptides. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Stiving%2C+Alyssa+Q%2E%22">Stiving, Alyssa Q.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Harvey%2C+Sophie+R%2E%22">Harvey, Sophie R.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Jones%2C+Benjamin+J%2E%22">Jones, Benjamin J.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Bellina%2C+Bruno%22">Bellina, Bruno</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Brown%2C+Jeffery+M%2E%22">Brown, Jeffery M.</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Barran%2C+Perdita+E%2E%22">Barran, Perdita E.</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Wysocki%2C+Vicki+H%2E%22">Wysocki, Vicki H.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> wysocki.11@osu.edu</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+the+American+Society+for+Mass+Spectrometry%22">Journal of the American Society for Mass Spectrometry</searchLink>. 11/4/2020, Vol. 31 Issue 11, p2313-2320. 8p. – Name: Abstract Label: Abstract Group: Ab Data: Ultraviolet photodissociation (UVPD) has emerged as a useful technique for characterizing peptide, protein, and protein complex primary and secondary structure. 193 nm UVPD, specifically, enables extensive covalent fragmentation of the peptide backbone without the requirement of a specific side chain chromophore and with no precursor charge state dependence. We have modified a commercial quadrupole-ion mobility-time-of-flight (Q-IM-TOF) mass spectrometer to include 193 nm UVPD following ion mobility. Ion mobility (IM) is a gas-phase separation technique that enables separation of ions by their size, shape, and charge, providing an orthogonal dimension of separation to mass analysis. Following instrument modifications, we characterized the performance of, and information that could be generated from, this new setup using the model peptides substance P, melittin, and insulin chain B. These experiments show extensive fragmentation across the peptide backbone and a variety of ion types as expected from 193 nm UVPD. Additionally, y-2 ions (along with complementary a+2 and b+2 ions) N-terminal to proline were observed. Combining the IM separation and mobility gating capabilities with UVPD, we demonstrate the ability to accomplish both mass- and mobility-selection of bradykinin des-Arg9 and des-Arg1 peptides followed by complete sequence characterization by UVPD. The new capabilities of this modified instrument demonstrate the utility of combining IM with UVPD because isobaric species cannot be independently selected with a traditional quadrupole alone. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Journal of the American Society for Mass Spectrometry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1021/jasms.0c00259 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 8 StartPage: 2313 Titles: – TitleFull: Coupling 193 nm Ultraviolet Photodissociation and Ion Mobility for Sequence Characterization of Conformationally-Selected Peptides. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Stiving, Alyssa Q. – PersonEntity: Name: NameFull: Harvey, Sophie R. – PersonEntity: Name: NameFull: Jones, Benjamin J. – PersonEntity: Name: NameFull: Bellina, Bruno – PersonEntity: Name: NameFull: Brown, Jeffery M. – PersonEntity: Name: NameFull: Barran, Perdita E. – PersonEntity: Name: NameFull: Wysocki, Vicki H. IsPartOfRelationships: – BibEntity: Dates: – D: 04 M: 11 Text: 11/4/2020 Type: published Y: 2020 Identifiers: – Type: issn-print Value: 10440305 Numbering: – Type: volume Value: 31 – Type: issue Value: 11 Titles: – TitleFull: Journal of the American Society for Mass Spectrometry Type: main |
| ResultId | 1 |
