Novel adsorptive polyamine coating for enhanced capillaryelectrophoresis of basic proteins and peptides
In capillary electrophoresis (CE), the anionic and hydrophobic nature of the fused-silica capillary surface has long been known to present a problem in protein and peptide analysis. The use of capillary surface coating is one of the approaches to avoid the analyte¿wall interactions. In this study, a...
| Autores: | , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2006 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/346592 |
| Acceso en línea: | http://hdl.handle.net/10261/346592 |
| Access Level: | acceso abierto |
| Palabra clave: | Capillary electrophoresis Polyamine coating Coated capillaries Proteins Peptides |
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Novel adsorptive polyamine coating for enhanced capillaryelectrophoresis of basic proteins and peptidesPuerta, Angel de laAxen, JakobSoderberg, LennartBergquist, JonasCapillary electrophoresisPolyamine coatingCoated capillariesProteinsPeptidesIn capillary electrophoresis (CE), the anionic and hydrophobic nature of the fused-silica capillary surface has long been known to present a problem in protein and peptide analysis. The use of capillary surface coating is one of the approaches to avoid the analyte¿wall interactions. In this study, a new polymer, poly-LA 313, has been synthesized, physico-chemical characterized, and applied as polyamine coating for CE separations. The coating process is highly reproducible and provides fast separations of peptides and proteins in a few minutes and with high efficiency. The physically adsorbed polymer gives rise to a durable coating in the range of pH 2¿10, in the presence of organic modifiers (acetonitrile and methanol) and with complex biological samples. The efficiency of the new cationic polymer was also tested performing protein and peptide separations with capillary electrophoresis-electrospray ionization-mass spectrometry (CE-ESI-MS).Angel Puerta acknowledges the Swedish Institute for a research grant. The Swedish Research Council is acknowledged for financial support(621-2002-5261,629-2002-6821J.B.).The authors acknowledges Prof. Ulf Hellman for help with the MALDI-MS measurements, G¨ oran Svensk for help with the Light Scattering measurements, Dr. Per Sj¨ oberg for help with the ESI-MS, and Dr. Sara Ullsten for fruitful discussions. Astra Zeneca and Agilent Technologies are acknowledged for the loan of the CE system and the MS system, respectively. Prof. Jonas Bergquist holds a senior research position financed by the Swedish Research Council.Peer reviewedElsevierSwedish InstituteConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2024202420062024info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/346592reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1016/j.jchromb.2006.04.018Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3465922026-05-22T06:33:51Z |
| dc.title.none.fl_str_mv |
Novel adsorptive polyamine coating for enhanced capillaryelectrophoresis of basic proteins and peptides |
| title |
Novel adsorptive polyamine coating for enhanced capillaryelectrophoresis of basic proteins and peptides |
| spellingShingle |
Novel adsorptive polyamine coating for enhanced capillaryelectrophoresis of basic proteins and peptides Puerta, Angel de la Capillary electrophoresis Polyamine coating Coated capillaries Proteins Peptides |
| title_short |
Novel adsorptive polyamine coating for enhanced capillaryelectrophoresis of basic proteins and peptides |
| title_full |
Novel adsorptive polyamine coating for enhanced capillaryelectrophoresis of basic proteins and peptides |
| title_fullStr |
Novel adsorptive polyamine coating for enhanced capillaryelectrophoresis of basic proteins and peptides |
| title_full_unstemmed |
Novel adsorptive polyamine coating for enhanced capillaryelectrophoresis of basic proteins and peptides |
| title_sort |
Novel adsorptive polyamine coating for enhanced capillaryelectrophoresis of basic proteins and peptides |
| dc.creator.none.fl_str_mv |
Puerta, Angel de la Axen, Jakob Soderberg, Lennart Bergquist, Jonas |
| author |
Puerta, Angel de la |
| author_facet |
Puerta, Angel de la Axen, Jakob Soderberg, Lennart Bergquist, Jonas |
| author_role |
author |
| author2 |
Axen, Jakob Soderberg, Lennart Bergquist, Jonas |
| author2_role |
author author author |
| dc.contributor.none.fl_str_mv |
Swedish Institute Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72] |
| dc.subject.none.fl_str_mv |
Capillary electrophoresis Polyamine coating Coated capillaries Proteins Peptides |
| topic |
Capillary electrophoresis Polyamine coating Coated capillaries Proteins Peptides |
| description |
In capillary electrophoresis (CE), the anionic and hydrophobic nature of the fused-silica capillary surface has long been known to present a problem in protein and peptide analysis. The use of capillary surface coating is one of the approaches to avoid the analyte¿wall interactions. In this study, a new polymer, poly-LA 313, has been synthesized, physico-chemical characterized, and applied as polyamine coating for CE separations. The coating process is highly reproducible and provides fast separations of peptides and proteins in a few minutes and with high efficiency. The physically adsorbed polymer gives rise to a durable coating in the range of pH 2¿10, in the presence of organic modifiers (acetonitrile and methanol) and with complex biological samples. The efficiency of the new cationic polymer was also tested performing protein and peptide separations with capillary electrophoresis-electrospray ionization-mass spectrometry (CE-ESI-MS). |
| publishDate |
2006 |
| dc.date.none.fl_str_mv |
2006 2024 2024 2024 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article http://purl.org/coar/resource_type/c_6501 Postprint info:eu-repo/semantics/acceptedVersion |
| format |
article |
| status_str |
acceptedVersion |
| dc.identifier.none.fl_str_mv |
http://hdl.handle.net/10261/346592 |
| url |
http://hdl.handle.net/10261/346592 |
| dc.language.none.fl_str_mv |
Inglés |
| language_invalid_str_mv |
Inglés |
| dc.relation.none.fl_str_mv |
http://dx.doi.org/10.1016/j.jchromb.2006.04.018 Sí |
| dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess |
| eu_rights_str_mv |
openAccess |
| dc.publisher.none.fl_str_mv |
Elsevier |
| publisher.none.fl_str_mv |
Elsevier |
| dc.source.none.fl_str_mv |
reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC instname:Consejo Superior de Investigaciones Científicas (CSIC) |
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Consejo Superior de Investigaciones Científicas (CSIC) |
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DIGITAL.CSIC. Repositorio Institucional del CSIC |
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DIGITAL.CSIC. Repositorio Institucional del CSIC |
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1869405129985228800 |
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15,198674 |