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Conformational antibody binding to a native, cell-free expressed GPCR in block copolymer membranes
- Source :
- PLoS ONE, Vol 9, Iss 10, p e110847 (2014), PLoS ONE
- Publication Year :
- 2014
- Publisher :
- Public Library of Science (PLoS), 2014.
-
Abstract
- G-protein coupled receptors (GPCRs) play a key role in physiological processes and are attractive drug targets. Their biophysical characterization is, however, highly challenging because of their innate instability outside a stabilizing membrane and the difficulty of finding a suitable expression system. We here show the cell-free expression of a GPCR, CXCR4, and its direct embedding in diblock copolymer membranes. The polymer-stabilized CXCR4 is readily immobilized onto biosensor chips for label-free binding analysis. Kinetic characterization using a conformationally sensitive antibody shows the receptor to exist in the correctly folded conformation, showing binding behaviour that is commensurate with heterologously expressed CXCR4. ASTAR (Agency for Sci., Tech. and Research, S’pore) Published version
- Subjects :
- Protein Folding
Protein Conformation
Cytokine Receptors
lcsh:Medicine
Synthetic Biotechnology
Biosensing Techniques
Protein Synthesis
Biochemistry
Immune Receptors
Receptor-Ligand Binding Assay
Mice
Binding Analysis
Protein structure
Copolymer
Receptor
lcsh:Science
Multidisciplinary
Immune System Proteins
Chemistry
Detectors
Nano-Enabled Synthetic Biology
Surface Plasmon Resonance Biosensor
Membrane
Physical Sciences
Engineering and Technology
Protein folding
Engineering::Materials::Biomaterials [DRNTU]
Research Article
Biotechnology
Receptors, CXCR4
Transmembrane Receptors
Immunology
Biophysics
Equipment
Research and Analysis Methods
Cell-Free Protein Synthesis
Antibodies
Animals
Humans
Chemical Characterization
G protein-coupled receptor
Cell-Free System
lcsh:R
Biology and Life Sciences
Proteins
Membranes, Artificial
Polymer Chemistry
Molecular biology
Monoclonal Antibodies
Biosensors
Membrane protein
Bionanotechnology
lcsh:Q
Biosensor
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 9
- Issue :
- 10
- Database :
- OpenAIRE
- Journal :
- PLoS ONE
- Accession number :
- edsair.doi.dedup.....c6ada90cebd3c8c7b2546af8c7cd340c