English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Activation of integrin function by nanopatterned adhesive interfaces

Arnold, M., Cavalcanti-Adam, E. A., Glass, R., Blümmel, J., Eck, W., Kantlehner, M., et al. (2004). Activation of integrin function by nanopatterned adhesive interfaces. ChemPhysChem, 5(3), 383-388. doi:10.1002/cphc.200301014.

Item is

Files

show Files
hide Files
:
ChemPhysChem_5_2004_383.pdf (Any fulltext), 196KB
 
File Permalink:
-
Name:
ChemPhysChem_5_2004_383.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
OA-Status:
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Arnold, Marco1, Author           
Cavalcanti-Adam, Elisabetta Ada1, 2, Author           
Glass, Roman1, Author           
Blümmel, Jacques1, Author           
Eck, Wolfgang, Author
Kantlehner, Martin, Author
Kessler, Horst, Author
Spatz, Joachim P.1, 2, Author           
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
2Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

Content

show
hide
Free keywords: cell adhesion; integrin; nanopatterning; self-assembly; surfaces
 Abstract: To study the function behind the molecular arrangement of single integrins in cell adhesion, we designed a hexagonally close-packed rigid template of cell-adhesive gold nanodots coated with cyclic RGDfK peptide by using block-copolymer micelle nanolithography. The diameter of the adhesive dots is < 8 nm, which allows the binding of one integrin per dot. These dots are positioned with high precision at 28, 58, 73, and 85 nm spacing at interfaces. A separation of > or = 73 nm between the adhesive dots results in limited cell attachment and spreading, and dramatically reduces the formation of focal adhesion and actin stress fibers. We attribute these cellular responses to restricted integrin clustering rather than insufficient number of ligand molecules in the cell-matrix interface since "micro-nanopatterned" substrates consisting of alternating fields with dense and no nanodots do support cell adhesion. We propose that the range between 58-73 nm is a universal length scale for integrin clustering and activation, since these properties are shared by a variety of cultured cells.

Details

show
hide
Language(s): eng - English
 Dates: 2003-10-172004-03-102004-03-19
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: ChemPhysChem
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Weinheim, Germany : Wiley-VCH
Pages: - Volume / Issue: 5 (3) Sequence Number: - Start / End Page: 383 - 388 Identifier: ISSN: 1439-4235
CoNE: https://pure.mpg.de/cone/journals/resource/954925409790