Ambient mass spectrometry (MS) methods such as desorption electrospray ionization-mass spectrometry (DESI-MS) provides direct ionization of analytes with little or no sample preparation. The capability for liquidsamples analysis allows DESI-MS to be coupled with many devices such as electrochemical cells and liquid chromatography (LC) for novel analytical applications. The online coupling of a thin-layer electrochemical flow cell with liquid sample DESI-MS can be applied for investigating different electrochemical reactions of biological molecules such as electrolytic reduction of disulfide-containing peptides/proteins. In addition, electrochemistry (EC) can assist the top-down characterization of proteins by electrolytic reduction of the disulfide bonds, in which sequence coverage can be significantly improved for electron-capture dissociation (ECD) and collision-induced dissociation (CID) analysis. Furthermore, the online coupling of LC with liquid sample DESI-MS was established, which allows a wide range of elution flow rates, online derivatization viareactive DESI to solve the post-column derivatization problems, also integration with EC. In addition, reactive DESI, which exploits the potential for coupling specific ion/molecule reactions with the ionization event, greatly improves the selectivity and efficiency for saccharide detection.
A systemic mass spectrometric investigation of a novel strategy for labeling biological thiols using selenamide reagents, involving the cleavage of the Se-N bond and form a new Se-S bond was introduced. Among 20 natural amino acids, the reaction is highly selective to thiol-containing peptides and proteins and occurs rapidly in high yield. The derivatization is also reversible upon additionof reducting reagents. The MS/MS dissociation behaviors of resulting peptide ions upon CID and electron-transfer dissociation (ETD) were investigated. In the positive ion mode, derivatized peptide ions exhibit tag-dependent CID dissociation pathways, allowing fast screening of peptides/proteins containing free cysteine residuesin a mixture. By contrast, ETD dissociation of the two selenamide-derivatized peptide ions show the facile loss of the tag, providing insight into the mechanism for electron-based ion dissociation. The derivatization reaction and related ion dissociation chemistry would find extensive applications in proteomics, including the derivatization of thiol protein/peptides arising from online electrolytic reduction mentioned above.
","abstract_html":"<p>Ambient mass spectrometry (MS) methods such as desorption electrospray ionization-mass spectrometry (DESI-MS) provides direct ionization of analytes with little or no sample preparation. The capability for liquidsamples analysis allows DESI-MS to be coupled with many devices such as electrochemical cells and liquid chromatography (LC) for novel analytical applications. The online coupling of a thin-layer electrochemical flow cell with liquid sample DESI-MS can be applied for investigating different electrochemical reactions of biological molecules such as electrolytic reduction of disulfide-containing peptides/proteins. In addition, electrochemistry (EC) can assist the top-down characterization of proteins by electrolytic reduction of the disulfide bonds, in which sequence coverage can be significantly improved for electron-capture dissociation (ECD) and collision-induced dissociation (CID) analysis. Furthermore, the online coupling of LC with liquid sample DESI-MS was established, which allows a wide range of elution flow rates, online derivatization viareactive DESI to solve the post-column derivatization problems, also integration with EC. In addition, reactive DESI, which exploits the potential for coupling specific ion/molecule reactions with the ionization event, greatly improves the selectivity and efficiency for saccharide detection. </p><p>A systemic mass spectrometric investigation of a novel strategy for labeling biological thiols using selenamide reagents, involving the cleavage of the Se-N bond and form a new Se-S bond was introduced. Among 20 natural amino acids, the reaction is highly selective to thiol-containing peptides and proteins and occurs rapidly in high yield. The derivatization is also reversible upon additionof reducting reagents. The MS/MS dissociation behaviors of resulting peptide ions upon CID and electron-transfer dissociation (ETD) were investigated. In the positive ion mode, derivatized peptide ions exhibit tag-dependent CID dissociation pathways, allowing fast screening of peptides/proteins containing free cysteine residuesin a mixture. By contrast, ETD dissociation of the two selenamide-derivatized peptide ions show the facile loss of the tag, providing insight into the mechanism for electron-based ion dissociation. The derivatization reaction and related ion dissociation chemistry would find extensive applications in proteomics, including the derivatization of thiol protein/peptides arising from online electrolytic reduction mentioned above.</p>","abstract_has_math":false,"creators":["Zhang, Yun"],"institution":"Ohio University","degree_name":"Doctor of Philosophy (PhD)","degree_level":"doctoral","degree_discipline":"Chemistry and Biochemistry (Arts and Sciences)","degree_department":null,"school":null,"contributors":["Chen, Hao"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2012,"date_issued":"2012","date_published":"2012","updated_at":"2026-07-24T03:35:52Z","subjects":["Chemistry","Mass spectrometry","Desorption electrospray ionization","Electrochemistry","Thiol derivatization","Disulfide bonds reduction","Top-down protein analysis"],"languages":["English"],"rights":["unrestricted","This thesis or dissertation is protected by copyright: all rights reserved. It may not be copied or redistributed beyond the terms of applicable copyright laws."],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1347395762","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Chen, Hao"]},{"key":"dc:creator","label":"Author","values":["Zhang, Yun"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2012"]},{"key":"dc:publisher","label":"Institution","values":["Ohio University / OhioLINK"]},{"key":"dc:type","label":"Dc Type","values":["Electronic Thesis or Dissertation"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry and Biochemistry (Arts and Sciences)"]},{"key":"thesis:degree_level","label":"Degree Level","values":["doctoral"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy (PhD)"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Ohio University"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry","Mass spectrometry","Desorption electrospray ionization","Electrochemistry","Thiol derivatization","Disulfide bonds reduction","Top-down protein analysis"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]},{"key":"dc:rights","label":"Dc Rights","values":["unrestricted","This thesis or dissertation is protected by copyright: all rights reserved. It may not be copied or redistributed beyond the terms of applicable copyright laws."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1347395762"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Ambient mass spectrometry (MS) methods such as desorption electrospray ionization-mass spectrometry (DESI-MS) provides direct ionization of analytes with little or no sample preparation. The capability for liquidsamples analysis allows DESI-MS to be coupled with many devices such as electrochemical cells and liquid chromatography (LC) for novel analytical applications. The online coupling of a thin-layer electrochemical flow cell with liquid sample DESI-MS can be applied for investigating different electrochemical reactions of biological molecules such as electrolytic reduction of disulfide-containing peptides/proteins. In addition, electrochemistry (EC) can assist the top-down characterization of proteins by electrolytic reduction of the disulfide bonds, in which sequence coverage can be significantly improved for electron-capture dissociation (ECD) and collision-induced dissociation (CID) analysis. Furthermore, the online coupling of LC with liquid sample DESI-MS was established, which allows a wide range of elution flow rates, online derivatization viareactive DESI to solve the post-column derivatization problems, also integration with EC. In addition, reactive DESI, which exploits the potential for coupling specific ion/molecule reactions with the ionization event, greatly improves the selectivity and efficiency for saccharide detection.
A systemic mass spectrometric investigation of a novel strategy for labeling biological thiols using selenamide reagents, involving the cleavage of the Se-N bond and form a new Se-S bond was introduced. Among 20 natural amino acids, the reaction is highly selective to thiol-containing peptides and proteins and occurs rapidly in high yield. The derivatization is also reversible upon additionof reducting reagents. The MS/MS dissociation behaviors of resulting peptide ions upon CID and electron-transfer dissociation (ETD) were investigated. In the positive ion mode, derivatized peptide ions exhibit tag-dependent CID dissociation pathways, allowing fast screening of peptides/proteins containing free cysteine residuesin a mixture. By contrast, ETD dissociation of the two selenamide-derivatized peptide ions show the facile loss of the tag, providing insight into the mechanism for electron-based ion dissociation. The derivatization reaction and related ion dissociation chemistry would find extensive applications in proteomics, including the derivatization of thiol protein/peptides arising from online electrolytic reduction mentioned above.
"]},{"key":"dc:format","label":"Dc Format","values":["application/pdf","3.77 MB"]},{"key":"dc:title","label":"Title","values":["Mass Spectrometric Analysis of Thiol Proteins/Peptides Following Selenamide Derivatization And Electrolytic Reduction of Disulfide Bonds"]}]}],"canonical_facts":{"dc:contributor":["Chen, Hao"],"dc:creator":["Zhang, Yun"],"dc:date":["2012"],"dc:description":["Ambient mass spectrometry (MS) methods such as desorption electrospray ionization-mass spectrometry (DESI-MS) provides direct ionization of analytes with little or no sample preparation. The capability for liquidsamples analysis allows DESI-MS to be coupled with many devices such as electrochemical cells and liquid chromatography (LC) for novel analytical applications. The online coupling of a thin-layer electrochemical flow cell with liquid sample DESI-MS can be applied for investigating different electrochemical reactions of biological molecules such as electrolytic reduction of disulfide-containing peptides/proteins. In addition, electrochemistry (EC) can assist the top-down characterization of proteins by electrolytic reduction of the disulfide bonds, in which sequence coverage can be significantly improved for electron-capture dissociation (ECD) and collision-induced dissociation (CID) analysis. Furthermore, the online coupling of LC with liquid sample DESI-MS was established, which allows a wide range of elution flow rates, online derivatization viareactive DESI to solve the post-column derivatization problems, also integration with EC. In addition, reactive DESI, which exploits the potential for coupling specific ion/molecule reactions with the ionization event, greatly improves the selectivity and efficiency for saccharide detection.
A systemic mass spectrometric investigation of a novel strategy for labeling biological thiols using selenamide reagents, involving the cleavage of the Se-N bond and form a new Se-S bond was introduced. Among 20 natural amino acids, the reaction is highly selective to thiol-containing peptides and proteins and occurs rapidly in high yield. The derivatization is also reversible upon additionof reducting reagents. The MS/MS dissociation behaviors of resulting peptide ions upon CID and electron-transfer dissociation (ETD) were investigated. In the positive ion mode, derivatized peptide ions exhibit tag-dependent CID dissociation pathways, allowing fast screening of peptides/proteins containing free cysteine residuesin a mixture. By contrast, ETD dissociation of the two selenamide-derivatized peptide ions show the facile loss of the tag, providing insight into the mechanism for electron-based ion dissociation. The derivatization reaction and related ion dissociation chemistry would find extensive applications in proteomics, including the derivatization of thiol protein/peptides arising from online electrolytic reduction mentioned above.
"],"dc:format":["application/pdf","3.77 MB"],"dc:identifier":["http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1347395762"],"dc:language":["English"],"dc:publisher":["Ohio University / OhioLINK"],"dc:rights":["unrestricted","This thesis or dissertation is protected by copyright: all rights reserved. It may not be copied or redistributed beyond the terms of applicable copyright laws."],"dc:subject":["Chemistry","Mass spectrometry","Desorption electrospray ionization","Electrochemistry","Thiol derivatization","Disulfide bonds reduction","Top-down protein analysis"],"dc:title":["Mass Spectrometric Analysis of Thiol Proteins/Peptides Following Selenamide Derivatization And Electrolytic Reduction of Disulfide Bonds"],"dc:type":["Electronic Thesis or Dissertation"],"thesis:degree_discipline":["Chemistry and Biochemistry (Arts and Sciences)"],"thesis:degree_level":["doctoral"],"thesis:degree_name":["Doctor of Philosophy (PhD)"],"thesis:institution_name":["Ohio University"]},"updated_at":"2026-07-24T03:35:52Z"}