ArticleProtein science : a publication of the Protein Society2002
Stable self-assembly of a protein engineering scaffold on gold surfaces.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 74 citations in OpenAlex.
- Formation of Tethered Bilayer Lipid Membranes (tBLMs) Using Plasma Membrane Blebs from Human Lung Cancer Cells.ACS omega · 2026Article
- Fully Aqueous Self-Assembly of a Gold-Nanoparticle-Based Pathogen Sensor.International journal of molecular sciences · 2023Article
- The Use of Tethered Bilayer Lipid Membranes to Identify the Mechanisms of Antimicrobial Peptide Interactions with Lipid Bilayers.Antibiotics (Basel, Switzerland) · 2019Review
- Engineered self-assembling monolayers for label free detection of influenza nucleoprotein.Biomedical microdevices · 2015Article
- High coverage fluid-phase floating lipid bilayers supported by ω-thiolipid self-assembled monolayers.Journal of the Royal Society, Interface · 2014Article
- Application of nanotechnology to control bacterial adhesion and patterning on material surfaces.Journal of experimental nanoscience · 2012Article
- Self-assembly of protein monolayers engineered for improved monoclonal immunoglobulin G binding.International journal of molecular sciences · 2011Article
- Advances in Bioconjugation.Current organic chemistry · 2010Article
- Neutrons for biologists: a beginner's guide, or why you should consider using neutrons.Journal of the Royal Society, Interface · 2009Review
- An ion-channel-containing model membrane: structural determination by magnetic contrast neutron reflectometry.Soft matter · 2009Article
- Monitoring the assembly of antibody-binding membrane protein arrays using polarised neutron reflection.European biophysics journal : EBJ · 2008Article
- A generic expression system to produce proteins that co-assemble with alkane thiol SAM.International journal of nanomedicine · 2008Article
- Covalent attachment of proteins to solid supports and surfaces via Sortase-mediated ligation.PloS one · 2007Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
The outer membrane protein OmpF from Escherichia coli is a member of a large family of beta-barrel membrane proteins. Some, like OmpF, are pore-forming proteins whilse others are active transporters or enzymes. We have previously shown that the receptor-binding domain (R-domain) of the toxin colicin N binds with high affinity to OmpF reconstituted into tethered lipid bilayers on gold electrodes. The binding can be measured by surface plasmon resonance (SPR) and ion channel blockage (impedance spectroscopy, IS). In this paper we report the use of a mutant OmpF-E183C in which a single cysteine had been introduced on a short periplasmic turn. OmpF-E183C binds directly to gold surfaces and creates high-density protein layers by self-assembly from detergent solution. When the gold surface is pretreated with beta-mercaptoethanol and thiolipids are added after the protein immobilisation step, the protein is shown, by Fourier transform infrared spectroscopy (FTIR), to retain its beta-rich structure. Furthermore, we could also measure R-domain binding by SPR and IS, confirming the functional reconstitution of a self-assembled membrane protein monolayer at the gold surface. Because these beta-barrel proteins are recognized protein engineering scaffolds, the method provides a generic method for the simple self-assembly of protein interfaces from aqueous solution.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.