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  Minimal synthetic cells to study integrin-mediated adhesion

Frohnmayer, J., Brüggemann, D., Eberhard, C., Neubauer, S., Mollenhauer, C., Böhm, H., et al. (2015). Minimal synthetic cells to study integrin-mediated adhesion. Angewandte Chemie International Edition in English, 54(42), 12472-12478. doi:10.1002/anie.201503184.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-DBB0-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-7DB0-B
Genre: Journal Article

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AngewChemIntEd_54_2015_12478.pdf (Any fulltext), 5MB
 
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 Creators:
Frohnmayer, Johannes1, 2, Author              
Brüggemann, Dorothea1, Author              
Eberhard, Christian1, 2, Author              
Neubauer, Stefanie, Author
Mollenhauer, Christine1, 2, Author              
Böhm, Heike1, 2, Author              
Kessler, Horst, Author
Geiger, Benjamin, 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              

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Free keywords: cell adhesion; integrin; liposomes; peptide mimetics; quartz crystal microbalance
 Abstract: To shed light on cell-adhesion-related molecular pathways, synthetic cells offer the unique advantage of a well-controlled model system with reduced molecular complexity. Herein, we show that liposomes with the reconstituted platelet integrin αIIb β3 as the adhesion-mediating transmembrane protein are a functional minimal cell model for studying cellular adhesion mechanisms in a defined environment. The interaction of these synthetic cells with various extracellular matrix proteins was analyzed using a quartz crystal microbalance with dissipation monitoring. The data indicated that integrin was functionally incorporated into the lipid vesicles, thus enabling integrin-specific adhesion of the engineered liposomes to fibrinogen- and fibronectin-functionalized surfaces. Then, we were able to initiate the detachment of integrin liposomes from these surfaces in the presence of the peptide GRGDSP, a process that is even faster with our newly synthesized peptide mimetic SN529, which specifically inhibits the integrin αIIb β3 .

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Language(s): eng - English
 Dates: 2015-05-282015-04-072015-08-072015-08-072015-10-12
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
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Title: Angewandte Chemie International Edition in English
  Other : Angewandte Chemie, International Edition in English
  Other : Angew. Chem., Int. Ed. Engl.
  Other : Angew. Chem. Int. Ed. Engl.
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 54 (42) Sequence Number: - Start / End Page: 12472 - 12478 Identifier: ISSN: 0570-0833
CoNE: https://pure.mpg.de/cone/journals/resource/0570-0833