Minimal synthetic cells to study integrin-mediated adhesion

• Verfasst von: Frohnmayer, Johannes [VerfasserIn]
• Verfasst von: Böhm, Heike [VerfasserIn]
• Verfasst von: Spatz, Joachim P. [VerfasserIn]
• Titel: Minimal synthetic cells to study integrin-mediated adhesion
• Verf.angabe: Johannes P. Frohnmayer, Dorothea Brüggemann, Christian Eberhard, Stefanie Neubauer, Christine Mollenhauer, Heike Boehm, Horst Kessler, Benjamin Geiger, and Joachim P. Spatz
• E-Jahr: 2015
• Jahr: 07 August 2015
• Umfang: 7 S.
• Teil: volume:54
• Teil: year:2015
• Teil: number:42
• Teil: pages:12472-12478
• Teil: extent:7
• Fussnoten: Gesehen am 05.08.2021
• Titel Quelle: Enthalten in: Angewandte Chemie / International edition
• Ort Quelle: Weinheim : Wiley-VCH, 1962
• Jahr Quelle: 2015
• Band/Heft Quelle: 54(2015), 42, Seite 12472-12478
• ISSN Quelle: 1521-3773
• DOI: doi:10.1002/anie.201503184
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: cell adhesion
• Sach-SW: integrin
• Sach-SW: liposomes
• Sach-SW: peptide mimetics
• Sach-SW: quartz crystal microbalance
• K10plus-PPN: 1765649633

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 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.