Journal Article FZJ-2016-05717

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Reconstitution of Fusion Proteins in Supported Lipid Bilayers for the Study of Cell Surface Receptor–Ligand Interactions in Cell–Cell Contact

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2016
ACS Publ. Washington, DC

Langmuir 32(14), 3462 - 3469 () [10.1021/acs.langmuir.5b04644]

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Abstract: Bioactive molecules such as adhesion ligands, growth factors, or enzymes play an important role in modulating cell behavior such as cell adhesion, spreading, and differentiation. Deciphering the mechanism of ligand-mediated cell adhesion and associated signaling is of great interest not only for fundamental biophysical investigations but also for applications in medicine and biotechnology. In the presented work, we developed a new biomimetic platform that enables culturing primary neurons and testing cell surface–receptor ligand interactions in cell–cell contacts as, e.g., in neuronal synapses. This platform consists of a supported lipid bilayer modified with incorporated neuronal adhesion proteins conjugated with the Fc-domain of IgG (ephrin A5 Fc-chimera). We extensively characterized properties of these protein containing bilayers using fluorescence recovery after photobleaching (FRAP), quartz crystal microbalance with dissipation (QCM-D), and immunostaining. We conclude that the Fc-domain is the part responsible for the incorporation of the protein into the bilayer. The biomimetic platform prepared by this new approach was able to promote neuronal cell adhesion and maintain growth as well as facilitate neuronal maturation as shown by electrophysiological measurements. We believe that our approach can be extended to insert other proteins to create a general culture platform for neurons and other cell types.

Classification:

Contributing Institute(s):
  1. Bioelektronik (ICS-8)
Research Program(s):
  1. 552 - Engineering Cell Function (POF3-552) (POF3-552)
  2. GRK 1572 - Bionik - Interaktionen über Grenzflächen zur Außenwelt (90190939) (90190939)

Appears in the scientific report 2016
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Medline ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; NationallizenzNationallizenz ; No Authors Fulltext ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection
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ICS > ICS-8
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 Record created 2016-11-02, last modified 2024-06-19


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