Water partial pressure X-ray photoelectron spectroscopy study of the conformation of fibrinogen on silanized hydrophilic/hydrophobic surfaces
Near ambient pressure X-ray photoelectron spectroscopy (NAP-XPS) allows the study of the conformational state of adsorbed proteins on surfaces at water partial pressures of a few mbar. In the present study, we used two organosilanes to prepare hydrophilic and hydrophobic surfaces. For the NAP-XPS st...
| Autores: | , , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2025 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/417374 |
| Acceso en línea: | http://hdl.handle.net/10261/417374 https://api.elsevier.com/content/abstract/scopus_id/105009277436 |
| Access Level: | acceso abierto |
| Palabra clave: | Conformation Fibrinogen H2O partial pressure Hydrophilic-hydrophobic NAP-XPS |
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Water partial pressure X-ray photoelectron spectroscopy study of the conformation of fibrinogen on silanized hydrophilic/hydrophobic surfacesFernández-Alonso, Francisco JavierCalvo, RodrigoSanz Calderón, AidaVillar-García, Ignacio J.Saiz, FernanHernando-Pérez, MercedesPérez Dieste, VirginiaManso Silván, MiguelConformationFibrinogenH2O partial pressureHydrophilic-hydrophobicNAP-XPSNear ambient pressure X-ray photoelectron spectroscopy (NAP-XPS) allows the study of the conformational state of adsorbed proteins on surfaces at water partial pressures of a few mbar. In the present study, we used two organosilanes to prepare hydrophilic and hydrophobic surfaces. For the NAP-XPS study, human fibrinogen, a sorbent serum protein with conformational dependent function, was adsorbed on contrasting surfaces, studied at 2 mbar H<inf>2</inf>O vapor pressure and compared with analysis at ultrahigh vacuum (UHV). Two different excitation energies were used to gain in-depth sensitivity. The C 1 s core level was fitted, and the components correlated with the presence of surface-exposed hydrophobic or hydrophilic moieties. The mode of analysis significantly affects the data on the conformation of fibrinogen on hydrophilic surfaces, showing surface-exposed (more intense) hydrophobic cues in the H<inf>2</inf>O NAP mode than in the UHV mode. Furthermore, the intensity of the C[sbnd]H peak exhibits the greatest variability in intensity, being more surface segregated on hydrophilic surfaces than on hydrophobic ones. The latter statement is sustained only for H<inf>2</inf>O NAP conditions, with no significant differences observed in the UHV mode. The work envisages greater sensitivity for forthcoming analyses of adsorbed proteins and other biomolecules by using water partial pressure XPS mode.The current research was funded through grants PID2020–112770RB-C22, PID2022–141080OB-C22, CNS2022–135285, PID2023–147200OB 100, PID2023–151371OB-C22, PID2023–151078OB-I00 and RyC2021–030929-I by MCIN/AEI/10.13039/501100011033 and European Union NextGenerationEU/PRTR. Additional funding from SI3/PJI/ 2021–00216 by Comunidad de Madrid and UAM is also acknowledged. FJFA acknowledges the Formación de Profesorado Universitario program, ref. FPU22/04365. Time allocated at ALBA synchrotron through 2020094555-BL24-CIRCE experiment is greatly appreciated.Peer reviewedElsevierMinisterio de Ciencia, Innovación y Universidades (España)European CommissionComunidad de MadridFernández-Alonso, Francisco Javier [0000-0002-7943-9328]Sanz Calderón, Aida [0000-0001-6185-653X]Saiz, Fernan [0000-0001-8565-8044]Manso Silván, Miguel [0000-0002-5063-1607]202620262025info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/417374https://api.elsevier.com/content/abstract/scopus_id/105009277436reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2020-112770RB-C22info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-141080OB-C22info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2023-147200OB-I00info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2023-151371OB-C22info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2023-151078OB-I00https://doi.org/10.1016/j.surfin.2025.106964Noinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/4173742026-05-22T06:33:51Z |
| dc.title.none.fl_str_mv |
Water partial pressure X-ray photoelectron spectroscopy study of the conformation of fibrinogen on silanized hydrophilic/hydrophobic surfaces |
| title |
Water partial pressure X-ray photoelectron spectroscopy study of the conformation of fibrinogen on silanized hydrophilic/hydrophobic surfaces |
| spellingShingle |
Water partial pressure X-ray photoelectron spectroscopy study of the conformation of fibrinogen on silanized hydrophilic/hydrophobic surfaces Fernández-Alonso, Francisco Javier Conformation Fibrinogen H2O partial pressure Hydrophilic-hydrophobic NAP-XPS |
| title_short |
Water partial pressure X-ray photoelectron spectroscopy study of the conformation of fibrinogen on silanized hydrophilic/hydrophobic surfaces |
| title_full |
Water partial pressure X-ray photoelectron spectroscopy study of the conformation of fibrinogen on silanized hydrophilic/hydrophobic surfaces |
| title_fullStr |
Water partial pressure X-ray photoelectron spectroscopy study of the conformation of fibrinogen on silanized hydrophilic/hydrophobic surfaces |
| title_full_unstemmed |
Water partial pressure X-ray photoelectron spectroscopy study of the conformation of fibrinogen on silanized hydrophilic/hydrophobic surfaces |
| title_sort |
Water partial pressure X-ray photoelectron spectroscopy study of the conformation of fibrinogen on silanized hydrophilic/hydrophobic surfaces |
| dc.creator.none.fl_str_mv |
Fernández-Alonso, Francisco Javier Calvo, Rodrigo Sanz Calderón, Aida Villar-García, Ignacio J. Saiz, Fernan Hernando-Pérez, Mercedes Pérez Dieste, Virginia Manso Silván, Miguel |
| author |
Fernández-Alonso, Francisco Javier |
| author_facet |
Fernández-Alonso, Francisco Javier Calvo, Rodrigo Sanz Calderón, Aida Villar-García, Ignacio J. Saiz, Fernan Hernando-Pérez, Mercedes Pérez Dieste, Virginia Manso Silván, Miguel |
| author_role |
author |
| author2 |
Calvo, Rodrigo Sanz Calderón, Aida Villar-García, Ignacio J. Saiz, Fernan Hernando-Pérez, Mercedes Pérez Dieste, Virginia Manso Silván, Miguel |
| author2_role |
author author author author author author author |
| dc.contributor.none.fl_str_mv |
Ministerio de Ciencia, Innovación y Universidades (España) European Commission Comunidad de Madrid Fernández-Alonso, Francisco Javier [0000-0002-7943-9328] Sanz Calderón, Aida [0000-0001-6185-653X] Saiz, Fernan [0000-0001-8565-8044] Manso Silván, Miguel [0000-0002-5063-1607] |
| dc.subject.none.fl_str_mv |
Conformation Fibrinogen H2O partial pressure Hydrophilic-hydrophobic NAP-XPS |
| topic |
Conformation Fibrinogen H2O partial pressure Hydrophilic-hydrophobic NAP-XPS |
| description |
Near ambient pressure X-ray photoelectron spectroscopy (NAP-XPS) allows the study of the conformational state of adsorbed proteins on surfaces at water partial pressures of a few mbar. In the present study, we used two organosilanes to prepare hydrophilic and hydrophobic surfaces. For the NAP-XPS study, human fibrinogen, a sorbent serum protein with conformational dependent function, was adsorbed on contrasting surfaces, studied at 2 mbar H<inf>2</inf>O vapor pressure and compared with analysis at ultrahigh vacuum (UHV). Two different excitation energies were used to gain in-depth sensitivity. The C 1 s core level was fitted, and the components correlated with the presence of surface-exposed hydrophobic or hydrophilic moieties. The mode of analysis significantly affects the data on the conformation of fibrinogen on hydrophilic surfaces, showing surface-exposed (more intense) hydrophobic cues in the H<inf>2</inf>O NAP mode than in the UHV mode. Furthermore, the intensity of the C[sbnd]H peak exhibits the greatest variability in intensity, being more surface segregated on hydrophilic surfaces than on hydrophobic ones. The latter statement is sustained only for H<inf>2</inf>O NAP conditions, with no significant differences observed in the UHV mode. The work envisages greater sensitivity for forthcoming analyses of adsorbed proteins and other biomolecules by using water partial pressure XPS mode. |
| publishDate |
2025 |
| dc.date.none.fl_str_mv |
2025 2026 2026 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article http://purl.org/coar/resource_type/c_6501 Publisher's version info:eu-repo/semantics/publishedVersion |
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article |
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publishedVersion |
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http://hdl.handle.net/10261/417374 https://api.elsevier.com/content/abstract/scopus_id/105009277436 |
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http://hdl.handle.net/10261/417374 https://api.elsevier.com/content/abstract/scopus_id/105009277436 |
| dc.relation.none.fl_str_mv |
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Elsevier |
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Elsevier |
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