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Minimal synthetic cells to study integrin-mediated adhesion

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 αIIbβ3 as the adhesion-mediating transmembrane protein ar...

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Bibliographic Details
Main Authors: Frohnmayer, Johannes (Author) , Böhm, Heike (Author) , Spatz, Joachim P. (Author)
Format: Article (Journal)
Language:English
Published: 07 August 2015
In: Angewandte Chemie. International edition
Year: 2015, Volume: 54, Issue: 42, Pages: 12472-12478
ISSN:1521-3773
DOI:10.1002/anie.201503184
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1002/anie.201503184
Verlag, lizenzpflichtig, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.201503184
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Author Notes:Johannes P. Frohnmayer, Dorothea Brüggemann, Christian Eberhard, Stefanie Neubauer, Christine Mollenhauer, Heike Boehm, Horst Kessler, Benjamin Geiger, and Joachim P. Spatz

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520 |a 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 αIIbβ3 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 αIIbβ3. 
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