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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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
07 August 2015
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| In: |
Angewandte Chemie. International edition
Year: 2015, Volume: 54, Issue: 42, Pages: 12472-12478 |
| ISSN: | 1521-3773 |
| DOI: | 10.1002/anie.201503184 |
| Online Access: | lizenzpflichtig lizenzpflichtig 
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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 |
| Summary: | 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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| Item Description: | Gesehen am 05.08.2021 |
| Physical Description: | Online Resource |
| ISSN: | 1521-3773 |
| DOI: | 10.1002/anie.201503184 |