ArticleBiochimica et biophysica acta2016
Global redesign of a native β-barrel scaffold.
Article in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Permeabilisation of the Outer Membrane of Escherichia coli for Enhanced Transport of Complex Molecules.Microbial biotechnology · 2025Article
- Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021Review
- Single-Molecule Protein Detection in a Biofluid Using a Quantitative Nanopore Sensor.ACS sensors · 2019Article
- High-Throughput Screening of Protein-Detergent Complexes Using Fluorescence Polarization Spectroscopy.Current protocols in protein science · 2019Article
- Kinetics of Membrane Protein-Detergent Interactions Depend on Protein Electrostatics.The journal of physical chemistry. B · 2018Article
- Detergent Desorption of Membrane Proteins Exhibits Two Kinetic Phases.The journal of physical chemistry letters · 2018Article
- Quantification of Membrane Protein-Detergent Complex Interactions.The journal of physical chemistry. B · 2017Article
- Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.Biochemistry · 2017Article
- Outer membrane protein design.Current opinion in structural biology · 2017Review
- Interrogating Detergent Desolvation of Nanopore-Forming Proteins by Fluorescence Polarization Spectroscopy.Analytical chemistry · 2017Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
One persistent challenge in membrane protein design is accomplishing extensive modifications of proteins without impairing their functionality. A truncation derivative of the ferric hydroxamate uptake component A (FhuA), which featured the deletion of the 160-residue cork domain and five large extracellular loops, produced the conversion of a non-conductive, monomeric, 22-stranded β-barrel protein into a large-conductance protein pore. Here, we show that this redesigned β-barrel protein tolerates an extensive alteration in the internal surface charge, encompassing 25 negative charge neutralizations. By using single-molecule electrophysiology, we noted that a commonality of various truncation FhuA protein pores was the occurrence of 33% blockades of the unitary current at very high transmembrane potentials. We determined that these current transitions were stimulated by their interaction with an external cationic polypeptide, which occurred in a fashion dependent on the surface charge of the pore interior as well as the polypeptide characteristics. This study shows promise for extensive engineering of a large monomeric β-barrel protein pore in molecular biomedical diagnosis, therapeutics, and biosensor technology.
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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.