On the molecular interaction between albumin and ib uprofen: An AFM and QCM D study

The adsorption of proteins on surfaces often results in a change of their structural behaviour and consequently, a loss of bioactivity. One experimental method to study interactions on a molecular level is single molecular force spectroscopy that permits to measure forces down to the pico-newton ran...

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Autores: Eleta López, Aitziber, Etxebarria, Juan, Reichardt, Niels Christian, Georgieva, Radostina, Bäumler, Hans, Toca Herrera, José Luis
Tipo de recurso: artículo
Fecha de publicación:2015
País:España
Institución:Universidad del País Vasco
Repositorio:Addi. Archivo Digital para la Docencia y la Investigación
OAI Identifier:oai:addi.ehu.eus:10810/76033
Acceso en línea:http://hdl.handle.net/10810/76033
Access Level:acceso abierto
Palabra clave:albumin
ibuprofen
unbinding force
atomic force microscopy
quartz crystal microbalance
protein functionality
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spelling On the molecular interaction between albumin and ib uprofen: An AFM and QCM D studyEleta López, AitziberEtxebarria, JuanReichardt, Niels ChristianGeorgieva, RadostinaBäumler, HansToca Herrera, José Luisalbuminibuprofenunbinding forceatomic force microscopyquartz crystal microbalanceprotein functionalityThe adsorption of proteins on surfaces often results in a change of their structural behaviour and consequently, a loss of bioactivity. One experimental method to study interactions on a molecular level is single molecular force spectroscopy that permits to measure forces down to the pico-newton range. In this work, the binding force between human serum albumin (HSA), covalently immobilized on glutaraldehyde modified gold substrates, and ibuprofen sodium salt was studied by means of single molecular force spectroscopy. First of all, a protocol was established to functionalize atomic force microscopy (AFM) tips with ibuprofen. The immobilization protocol was additionally tested by quartz crystal microbalance with dissipation (QCM-D) and contact angle measurements. AFM was used to characterize the adsorption of HSA on gold substrates, which lead to a packed monolayer of thickness slightly lower than the reported value in solution. Finally, single molecule spectroscopy results were used to characterize the binding force between albumin and ibuprofen and calculate the distance of the transition state (0.6 nm) and the dissociation rate constant (0.055 s-1). The results might indicate that part of the adsorbed protein still preserves its functionality upon adsorption.The authors thank the Etortek program of the Basque government (07/27 [IE07/201]) and the Spanish Ministry of Education and Science (grant CTQ2007-66541).Elsevier202520252015info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10810/76033reponame:Addi. Archivo Digital para la Docencia y la Investigacióninstname:Universidad del País VascoIngléshttps://doi.org/10.1016/j.colsurfb.2015.06.063info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/4.0/© 2015 Elsevier under CC BY-NC-ND licenseoai:addi.ehu.eus:10810/760332026-06-18T09:23:17Z
dc.title.none.fl_str_mv On the molecular interaction between albumin and ib uprofen: An AFM and QCM D study
title On the molecular interaction between albumin and ib uprofen: An AFM and QCM D study
spellingShingle On the molecular interaction between albumin and ib uprofen: An AFM and QCM D study
Eleta López, Aitziber
albumin
ibuprofen
unbinding force
atomic force microscopy
quartz crystal microbalance
protein functionality
title_short On the molecular interaction between albumin and ib uprofen: An AFM and QCM D study
title_full On the molecular interaction between albumin and ib uprofen: An AFM and QCM D study
title_fullStr On the molecular interaction between albumin and ib uprofen: An AFM and QCM D study
title_full_unstemmed On the molecular interaction between albumin and ib uprofen: An AFM and QCM D study
title_sort On the molecular interaction between albumin and ib uprofen: An AFM and QCM D study
dc.creator.none.fl_str_mv Eleta López, Aitziber
Etxebarria, Juan
Reichardt, Niels Christian
Georgieva, Radostina
Bäumler, Hans
Toca Herrera, José Luis
author Eleta López, Aitziber
author_facet Eleta López, Aitziber
Etxebarria, Juan
Reichardt, Niels Christian
Georgieva, Radostina
Bäumler, Hans
Toca Herrera, José Luis
author_role author
author2 Etxebarria, Juan
Reichardt, Niels Christian
Georgieva, Radostina
Bäumler, Hans
Toca Herrera, José Luis
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv albumin
ibuprofen
unbinding force
atomic force microscopy
quartz crystal microbalance
protein functionality
topic albumin
ibuprofen
unbinding force
atomic force microscopy
quartz crystal microbalance
protein functionality
description The adsorption of proteins on surfaces often results in a change of their structural behaviour and consequently, a loss of bioactivity. One experimental method to study interactions on a molecular level is single molecular force spectroscopy that permits to measure forces down to the pico-newton range. In this work, the binding force between human serum albumin (HSA), covalently immobilized on glutaraldehyde modified gold substrates, and ibuprofen sodium salt was studied by means of single molecular force spectroscopy. First of all, a protocol was established to functionalize atomic force microscopy (AFM) tips with ibuprofen. The immobilization protocol was additionally tested by quartz crystal microbalance with dissipation (QCM-D) and contact angle measurements. AFM was used to characterize the adsorption of HSA on gold substrates, which lead to a packed monolayer of thickness slightly lower than the reported value in solution. Finally, single molecule spectroscopy results were used to characterize the binding force between albumin and ibuprofen and calculate the distance of the transition state (0.6 nm) and the dissociation rate constant (0.055 s-1). The results might indicate that part of the adsorbed protein still preserves its functionality upon adsorption.
publishDate 2015
dc.date.none.fl_str_mv 2015
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10810/76033
url http://hdl.handle.net/10810/76033
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://doi.org/10.1016/j.colsurfb.2015.06.063
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/4.0/
© 2015 Elsevier under CC BY-NC-ND license
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
© 2015 Elsevier under CC BY-NC-ND license
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Addi. Archivo Digital para la Docencia y la Investigación
instname:Universidad del País Vasco
instname_str Universidad del País Vasco
reponame_str Addi. Archivo Digital para la Docencia y la Investigación
collection Addi. Archivo Digital para la Docencia y la Investigación
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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