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    
Abstract/OtherAbstract:
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.
Authors:
Noriko Tomita; Mohammad M Mohammad; David J Niedzwiecki; Makoto Ohta; Liviu Movileanu
Related Documents :
7448236 - Selective action of colchicine on protein synthesis and release in a clonal line of rat...
23000216 - 2,2,2-trifluoroethyl 6-thio-β-d-glucopyranoside as a selective tag for cysteines in pro...
24321316 - Role of rac gtpase activating proteins in regulation of nadph oxidase in human neutroph...
23872606 - The roles of moonlighting proteins in bacteria.
23806606 - Advances in multiplexed mrm-based protein biomarker quantitation toward clinical utility.
22627026 - Shared features of s100b immunohistochemistry and cytochrome oxidase histochemistry in ...
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.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Bacterial Outer Membrane Proteins / chemistry*,  metabolism
Biophysics / methods
Biosensing Techniques
Electric Conductivity
Electrophysiology
Escherichia coli / metabolism
Escherichia coli Proteins / chemistry*,  metabolism
Hydrogen-Ion Concentration
Lipid Bilayers / chemistry
Lipids / chemistry*
Membrane Potentials
Molecular Conformation
Nanoparticles / chemistry
Nanopores*
Nanotechnology / methods
Protein Engineering / methods*
Protein Structure, Secondary
Grant Support
ID/Acronym/Agency:
R01 GM088403/GM/NIGMS NIH HHS; R01 GM088403/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Outer Membrane Proteins; 0/Escherichia coli Proteins; 0/FhuA protein, E coli; 0/Lipid Bilayers; 0/Lipids
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Effect of post-exercise hydrotherapy water temperature on subsequent exhaustive running performance ...
Next Document:  The p7 protein of the hepatitis C virus induces cell death differently from the influenza A virus vi...