Document Detail

Does the lipid environment impact the open-state conductance of an engineered β-barrel protein nanopore?
MedLine Citation:
PMID:  23246446     Owner:  NLM     Status:  MEDLINE    
Using rational membrane protein design, we were recently able to obtain a β-barrel protein nanopore that was robust under an unusually broad range of experimental circumstances. This protein nanopore was based upon the native scaffold of the bacterial ferric hydroxamate uptake component A (FhuA) of Escherichia coli. In this work, we expanded the examinations of the open-state current of this engineered protein nanopore, also called FhuA ΔC/Δ4L, employing an array of lipid bilayer systems that contained charged and uncharged as well as conical and cylindrical lipids. Remarkably, systematical single-channel analysis of FhuA ΔC/Δ4L indicated that most of its biophysical features, such as the unitary conductance and the stability of the open-state current, were not altered under the conditions tested in this work. However, electrical recordings at high transmembrane potentials revealed that the presence of conical phospholipids within the bilayer catalyzes the first, stepwise current transition of the FhuA ΔC/Δ4L protein nanopore to a lower-conductance open state. This study reinforces the stability of the open-state current of the engineered FhuA ΔC/Δ4L protein nanopore under various experimental conditions, paving the way for further critical developments in biosensing and molecular biomedical diagnosis.
Noriko Tomita; Mohammad M Mohammad; David J Niedzwiecki; Makoto Ohta; Liviu Movileanu
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-12-11
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1828     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-01-30     Completed Date:  2013-04-08     Revised Date:  2014-03-07    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  1057-65     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier B.V. All rights reserved.
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MeSH Terms
Bacterial Outer Membrane Proteins / chemistry*,  metabolism
Biophysics / methods
Biosensing Techniques
Electric Conductivity
Escherichia coli / metabolism
Escherichia coli Proteins / chemistry*,  metabolism
Hydrogen-Ion Concentration
Lipid Bilayers / chemistry
Lipids / chemistry*
Membrane Potentials
Molecular Conformation
Nanoparticles / chemistry
Nanotechnology / methods
Protein Engineering / methods*
Protein Structure, Secondary
Grant Support
Reg. No./Substance:
0/Bacterial Outer Membrane Proteins; 0/Escherichia coli Proteins; 0/FhuA protein, E coli; 0/Lipid Bilayers; 0/Lipids

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