Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell Adhesion

Autores
Pallarola, Diego Andres; Bochen, Alexander; Boehm, Heike; Rechenmacher, Florian; Sobahi, Tarik R.; Spatz, Joachim P.; Kessler, Horst
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The interaction of specifi c surface receptors of the integrin family with different extracellular matrix-based ligands is of utmost importance for the cellular adhesion process. A ligand consists of an integrin-binding group, here cyclic RGDfX, a spacer molecule that lifts the integrin-binding group from the surface and a surface anchoring group. c (-RGDfX-) peptides are bound to gold nanoparticle structured surfaces via polyproline, polyethylene glycol or aminohexanoic acid containing spacers of different lengths. Although keeping the integrin-binding c (-RGDfX-) peptides constant for all compounds, changes of the ligand´s spacer chemistry and length reveal signifi cant differences in cell adhesion activation and focal adhesion formation. Polyproline-based peptides demonstrate improved cell adhesion kinetics and focal adhesion formation compared with common aminohexanoic acid or polyethylene glycol spacers. Binding activity can additionally be improved by applying ligands with two head groups, inducing a multimeric effect. This study gives insights into spacer-based differences in integrin-driven cell adhesion processes and remarkably highlights the polyproline-based spacers as suitable ligand-presenting templates for surface functionalization.
Fil: Pallarola, Diego Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina. Max Planck Institute for intelligent Systems; Alemania. University of Heidelberg; Alemania
Fil: Bochen, Alexander. Universitat Technical Zu Munich; Alemania. Max Planck Institute for intelligent Systems; Alemania
Fil: Boehm, Heike. Max Planck Institute for intelligent Systems; Alemania. University of Heidelberg; Alemania
Fil: Rechenmacher, Florian. Universitat Technical Zu Munich; Alemania
Fil: Sobahi, Tarik R.. King Abdulaziz University; Arabia Saudita
Fil: Spatz, Joachim P.. Max Planck Institute for intelligent Systems; Alemania. University of Heidelberg; Alemania
Fil: Kessler, Horst. Universitat Technical Zu Munich; Alemania
Materia
CELL ADHESION
CYCLIC RGD
INTEGRINS
NANOSTRUCTURED SURFACES
POLYPROLINE SPACER
POLYETHYLENEGLYCOL SPACER
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/5101
Acceder
id CONICETDig_3c805f16bca82f7795934e025d9960a7
oai_identifier_str oai:ri.conicet.gov.ar:11336/5101
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell AdhesionPallarola, Diego AndresBochen, AlexanderBoehm, HeikeRechenmacher, FlorianSobahi, Tarik R.Spatz, Joachim P.Kessler, HorstCELL ADHESIONCYCLIC RGDINTEGRINSNANOSTRUCTURED SURFACESPOLYPROLINE SPACERPOLYETHYLENEGLYCOL SPACERhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1https://purl.org/becyt/ford/2.10https://purl.org/becyt/ford/2https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The interaction of specifi c surface receptors of the integrin family with different extracellular matrix-based ligands is of utmost importance for the cellular adhesion process. A ligand consists of an integrin-binding group, here cyclic RGDfX, a spacer molecule that lifts the integrin-binding group from the surface and a surface anchoring group. c (-RGDfX-) peptides are bound to gold nanoparticle structured surfaces via polyproline, polyethylene glycol or aminohexanoic acid containing spacers of different lengths. Although keeping the integrin-binding c (-RGDfX-) peptides constant for all compounds, changes of the ligand´s spacer chemistry and length reveal signifi cant differences in cell adhesion activation and focal adhesion formation. Polyproline-based peptides demonstrate improved cell adhesion kinetics and focal adhesion formation compared with common aminohexanoic acid or polyethylene glycol spacers. Binding activity can additionally be improved by applying ligands with two head groups, inducing a multimeric effect. This study gives insights into spacer-based differences in integrin-driven cell adhesion processes and remarkably highlights the polyproline-based spacers as suitable ligand-presenting templates for surface functionalization.Fil: Pallarola, Diego Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina. Max Planck Institute for intelligent Systems; Alemania. University of Heidelberg; AlemaniaFil: Bochen, Alexander. Universitat Technical Zu Munich; Alemania. Max Planck Institute for intelligent Systems; AlemaniaFil: Boehm, Heike. Max Planck Institute for intelligent Systems; Alemania. University of Heidelberg; AlemaniaFil: Rechenmacher, Florian. Universitat Technical Zu Munich; AlemaniaFil: Sobahi, Tarik R.. King Abdulaziz University; Arabia SauditaFil: Spatz, Joachim P.. Max Planck Institute for intelligent Systems; Alemania. University of Heidelberg; AlemaniaFil: Kessler, Horst. Universitat Technical Zu Munich; AlemaniaWiley2014-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/5101Pallarola, Diego Andres; Bochen, Alexander; Boehm, Heike; Rechenmacher, Florian; Sobahi, Tarik R.; et al.; Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell Adhesion; Wiley; Advanced Functional Materials; 24; 7; 3-2014; 943-9561616-301Xenginfo:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4368046/info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/adfm.201302411/abstractinfo:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/altIdentifier/doi/10.1002/adfm.201302411info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:22:00Zoai:ri.conicet.gov.ar:11336/5101instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-10 13:22:00.683CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell Adhesion
title Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell Adhesion
spellingShingle Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell Adhesion
Pallarola, Diego Andres
CELL ADHESION
CYCLIC RGD
INTEGRINS
NANOSTRUCTURED SURFACES
POLYPROLINE SPACER
POLYETHYLENEGLYCOL SPACER
title_short Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell Adhesion
title_full Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell Adhesion
title_fullStr Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell Adhesion
title_full_unstemmed Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell Adhesion
title_sort Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell Adhesion
dc.creator.none.fl_str_mv Pallarola, Diego Andres
Bochen, Alexander
Boehm, Heike
Rechenmacher, Florian
Sobahi, Tarik R.
Spatz, Joachim P.
Kessler, Horst
author Pallarola, Diego Andres
author_facet Pallarola, Diego Andres
Bochen, Alexander
Boehm, Heike
Rechenmacher, Florian
Sobahi, Tarik R.
Spatz, Joachim P.
Kessler, Horst
author_role author
author2 Bochen, Alexander
Boehm, Heike
Rechenmacher, Florian
Sobahi, Tarik R.
Spatz, Joachim P.
Kessler, Horst
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv CELL ADHESION
CYCLIC RGD
INTEGRINS
NANOSTRUCTURED SURFACES
POLYPROLINE SPACER
POLYETHYLENEGLYCOL SPACER
topic CELL ADHESION
CYCLIC RGD
INTEGRINS
NANOSTRUCTURED SURFACES
POLYPROLINE SPACER
POLYETHYLENEGLYCOL SPACER
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/2.10
https://purl.org/becyt/ford/2
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The interaction of specifi c surface receptors of the integrin family with different extracellular matrix-based ligands is of utmost importance for the cellular adhesion process. A ligand consists of an integrin-binding group, here cyclic RGDfX, a spacer molecule that lifts the integrin-binding group from the surface and a surface anchoring group. c (-RGDfX-) peptides are bound to gold nanoparticle structured surfaces via polyproline, polyethylene glycol or aminohexanoic acid containing spacers of different lengths. Although keeping the integrin-binding c (-RGDfX-) peptides constant for all compounds, changes of the ligand´s spacer chemistry and length reveal signifi cant differences in cell adhesion activation and focal adhesion formation. Polyproline-based peptides demonstrate improved cell adhesion kinetics and focal adhesion formation compared with common aminohexanoic acid or polyethylene glycol spacers. Binding activity can additionally be improved by applying ligands with two head groups, inducing a multimeric effect. This study gives insights into spacer-based differences in integrin-driven cell adhesion processes and remarkably highlights the polyproline-based spacers as suitable ligand-presenting templates for surface functionalization.
Fil: Pallarola, Diego Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina. Max Planck Institute for intelligent Systems; Alemania. University of Heidelberg; Alemania
Fil: Bochen, Alexander. Universitat Technical Zu Munich; Alemania. Max Planck Institute for intelligent Systems; Alemania
Fil: Boehm, Heike. Max Planck Institute for intelligent Systems; Alemania. University of Heidelberg; Alemania
Fil: Rechenmacher, Florian. Universitat Technical Zu Munich; Alemania
Fil: Sobahi, Tarik R.. King Abdulaziz University; Arabia Saudita
Fil: Spatz, Joachim P.. Max Planck Institute for intelligent Systems; Alemania. University of Heidelberg; Alemania
Fil: Kessler, Horst. Universitat Technical Zu Munich; Alemania
description The interaction of specifi c surface receptors of the integrin family with different extracellular matrix-based ligands is of utmost importance for the cellular adhesion process. A ligand consists of an integrin-binding group, here cyclic RGDfX, a spacer molecule that lifts the integrin-binding group from the surface and a surface anchoring group. c (-RGDfX-) peptides are bound to gold nanoparticle structured surfaces via polyproline, polyethylene glycol or aminohexanoic acid containing spacers of different lengths. Although keeping the integrin-binding c (-RGDfX-) peptides constant for all compounds, changes of the ligand´s spacer chemistry and length reveal signifi cant differences in cell adhesion activation and focal adhesion formation. Polyproline-based peptides demonstrate improved cell adhesion kinetics and focal adhesion formation compared with common aminohexanoic acid or polyethylene glycol spacers. Binding activity can additionally be improved by applying ligands with two head groups, inducing a multimeric effect. This study gives insights into spacer-based differences in integrin-driven cell adhesion processes and remarkably highlights the polyproline-based spacers as suitable ligand-presenting templates for surface functionalization.
publishDate 2014
dc.date.none.fl_str_mv 2014-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/5101
Pallarola, Diego Andres; Bochen, Alexander; Boehm, Heike; Rechenmacher, Florian; Sobahi, Tarik R.; et al.; Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell Adhesion; Wiley; Advanced Functional Materials; 24; 7; 3-2014; 943-956
1616-301X
url http://hdl.handle.net/11336/5101
identifier_str_mv Pallarola, Diego Andres; Bochen, Alexander; Boehm, Heike; Rechenmacher, Florian; Sobahi, Tarik R.; et al.; Interface Immobilization Chemistry of c RGD-based Peptides Regulates Integrin Mediated Cell Adhesion; Wiley; Advanced Functional Materials; 24; 7; 3-2014; 943-956
1616-301X
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4368046/
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/adfm.201302411/abstract
info:eu-repo/semantics/altIdentifier/doi/
info:eu-repo/semantics/altIdentifier/doi/10.1002/adfm.201302411
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.48226

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