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Homotrimeric Collagen Peptides As Model Systems For Cell Adhesion Studies

  • Leslie Barth
  • Eva K. Sinner
  • Sergio A. Cadamuro
  • Christian Renner
  • Dieter Oesterhelt
  • Luis Moroder
Part of the Advances in Experimental Medicine and Biology book series (volume 611)

Germany

Collagen model peptides with high triple-helix propensity can self-associate into the suprahelical structure, but folding/unfolding of such systems is strongly concentration-dependent. Cross-bridging of the three collagenous chains with synthetic templates as well as with native collagen-type or with artificial cystine knots has been successfully applied to overcome the shortcomings of self-assembled triple helices [1]. Aim of the present study was to analyze the conformational properties of a disulfide-crosslinked trimeric collagen model peptide (2 in Figure 1) containing the specific collagen type I motif recognized by the α1β1 and α2β1 integrins i.e. the hexapeptide sequence portion GFOGER of the α1 chain [2]. Embedding this adhesion epitope into the triple helical collagenous peptide 3 (Figure 1) allowed X-ray structural analysis of the complex with the α2-I domain, which provides within the α2β 1 integrin the principal binding site for collagen [3].

Keywords

Triple Helix Collagen Peptide Basal Membrane Collagen Adhesion Motif Cell Adhesion Study 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Notes

Acknowledgments

The work was funded by the SFB 563 (grant C4) of the DFG.

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Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  • Leslie Barth
    • 1
  • Eva K. Sinner
    • 1
  • Sergio A. Cadamuro
    • 1
  • Christian Renner
    • 1
  • Dieter Oesterhelt
    • 1
  • Luis Moroder
    • 1
  1. 1.Max-Planck-Institute of BiochemistryMartinsriedGermany

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