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

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 grou...

Descripción completa

Detalles Bibliográficos
Autores principales: Pallarola, Diego Andrés, Bochen, Alexander, Boehm, Heike, Rechenmacher, Florian, Sobahi, Tarik R., Spatz, Joachim P., Kessler, Horst
Formato: Articulo
Lenguaje:Inglés
Publicado: 2014
Materias:
Ciencias Exactas
Química
cell adhesion
cyclic RGD
integrins
nanostructured surfaces
polyproline spacer
polyethyleneglycol spacer
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/104763
http://hdl.handle.net/11336/5101
http://onlinelibrary.wiley.com/doi/10.1002/adfm.201302411/abstract
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-104763
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Química
cell adhesion
cyclic RGD
integrins
nanostructured surfaces
polyproline spacer
polyethyleneglycol spacer
spellingShingle Ciencias Exactas
Química
cell adhesion
cyclic RGD
integrins
nanostructured surfaces
polyproline spacer
polyethyleneglycol spacer
Pallarola, Diego Andrés
Bochen, Alexander
Boehm, Heike
Rechenmacher, Florian
Sobahi, Tarik R.
Spatz, Joachim P.
Kessler, Horst
Interface Immobilization Chemistry of cRGD-based Peptides Regulates Integrin Mediated Cell Adhesion
topic_facet Ciencias Exactas
Química
cell adhesion
cyclic RGD
integrins
nanostructured surfaces
polyproline spacer
polyethyleneglycol spacer
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.
format Articulo
Articulo
author Pallarola, Diego Andrés
Bochen, Alexander
Boehm, Heike
Rechenmacher, Florian
Sobahi, Tarik R.
Spatz, Joachim P.
Kessler, Horst
author_facet Pallarola, Diego Andrés
Bochen, Alexander
Boehm, Heike
Rechenmacher, Florian
Sobahi, Tarik R.
Spatz, Joachim P.
Kessler, Horst
author_sort Pallarola, Diego Andrés
title Interface Immobilization Chemistry of cRGD-based Peptides Regulates Integrin Mediated Cell Adhesion
title_short Interface Immobilization Chemistry of cRGD-based Peptides Regulates Integrin Mediated Cell Adhesion
title_full Interface Immobilization Chemistry of cRGD-based Peptides Regulates Integrin Mediated Cell Adhesion
title_fullStr Interface Immobilization Chemistry of cRGD-based Peptides Regulates Integrin Mediated Cell Adhesion
title_full_unstemmed Interface Immobilization Chemistry of cRGD-based Peptides Regulates Integrin Mediated Cell Adhesion
title_sort interface immobilization chemistry of crgd-based peptides regulates integrin mediated cell adhesion
publishDate 2014
url http://sedici.unlp.edu.ar/handle/10915/104763
http://hdl.handle.net/11336/5101
http://onlinelibrary.wiley.com/doi/10.1002/adfm.201302411/abstract
work_keys_str_mv AT pallaroladiegoandres interfaceimmobilizationchemistryofcrgdbasedpeptidesregulatesintegrinmediatedcelladhesion
AT bochenalexander interfaceimmobilizationchemistryofcrgdbasedpeptidesregulatesintegrinmediatedcelladhesion
AT boehmheike interfaceimmobilizationchemistryofcrgdbasedpeptidesregulatesintegrinmediatedcelladhesion
AT rechenmacherflorian interfaceimmobilizationchemistryofcrgdbasedpeptidesregulatesintegrinmediatedcelladhesion
AT sobahitarikr interfaceimmobilizationchemistryofcrgdbasedpeptidesregulatesintegrinmediatedcelladhesion
AT spatzjoachimp interfaceimmobilizationchemistryofcrgdbasedpeptidesregulatesintegrinmediatedcelladhesion
AT kesslerhorst interfaceimmobilizationchemistryofcrgdbasedpeptidesregulatesintegrinmediatedcelladhesion
bdutipo_str Repositorios
_version_ 1764820442312343553

Ejemplares similares