English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Focal adhesion stabilization by enhanced integrin-cRGD binding affinity

Pallarola, D., Platzman, I., Bochen, A., Cavalcanti-Adam, E. A., Axmann, M., Kessler, H., et al. (2017). Focal adhesion stabilization by enhanced integrin-cRGD binding affinity. BioNanoMaterials, 18(1-2): 20160014, pp. 1-13. doi:10.1515/bnm-2016-0014.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-C70D-E Version Permalink: http://hdl.handle.net/21.11116/0000-0000-2D14-8
Genre: Journal Article

Files

show Files
hide Files
:
BioNanoMat_18_2017_20160014.pdf (Any fulltext), 996KB
 
File Permalink:
-
Name:
BioNanoMat_18_2017_20160014.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Pallarola, Diego1, 2, Author              
Platzman, Ilia1, 2, Author              
Bochen, Alexander, Author
Cavalcanti-Adam, Elisabetta Ada1, 2, Author              
Axmann, Markus, Author
Kessler, Horst, Author
Geiger, Benjamin, Author
Spatz, Joachim P.1, 2, Author              
Affiliations:
1Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              
2Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              

Content

show
hide
Free keywords: biointerfaces; cell adhesion; cyclic RGD; integrins; ligand binding affinity; polyproline spacer
 Abstract: In this study we investigate the impact of ligand presentation by various molecular spacers on integrin-based focal adhesion formation. Gold nanoparticles (AuNPs) arranged in hexagonal patterns were biofunctionalized with the same ligand head group, cyclic Arg-Gly-Asp [c(-RGDfX-)], but with different molecular spacers, each of which couples the head group to the gold. Aminohexanoic acid, polyethylene glycol (PEG) and polyproline spacers were used to vary the distance between the binding motif and the substrate, and thus the presentation of integrin binding on anchoring points. Adherent cells plated on nanopatterned surfaces with polyproline spacers for peptide immobilization could tolerate larger ligand spacing (162 nm) for focal adhesion formation, in comparison to cells on surfaces with PEG (110 nm) or aminohexanoic acid (62 nm) spacers. Due to the rigidity of the polyproline spacer, enhanced access to the ligand-binding site upon integrin-cRGD complex formation increases the probability of rebinding and decreases unbinding, as measured by fluorescence recovery after photobleaching (FRAP) analysis, compared to the analogues with aminohexanoic acid or PEG-containing spacers. These findings indicate that focal adhesion formation may not only be stabilized upon tight integrin clustering, but also by tuning the efficiency of the exposure of the cRGD-based ligand to the integrin extracellular domains. Our studies clearly highlight the importance of ligand spatial presentation for regulating adhesion-dependent cell behavior, and provide a sound approach for studying cell signaling processes on nanometer-scale, engineered bioactive surfaces under chemical stimuli of varying intensities.

Details

show
hide
Language(s): eng - English
 Dates: 2016-10-242017-01-192017-02-23
 Publication Status: Published online
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1515/bnm-2016-0014
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: BioNanoMaterials
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Berlin, Germany : Walter de Gruyter
Pages: - Volume / Issue: 18 (1-2) Sequence Number: 20160014 Start / End Page: 1 - 13 Identifier: ISSN: 2193-066X
CoNE: https://pure.mpg.de/cone/journals/resource/2193-066X