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Discrimination of supramolecular chirality using a protein nanopore

Supramolecular chirality may emerge from self-assembly processes to yield architectures that differ only in the topological arrangement of their constituent parts. Since the properties of the resulting enantiomeric assemblies are identical, purification and characterisation can be challenging. Here,...

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Detalles Bibliográficos
Autores principales: Cooper, James A., Borsley, Stefan, Lusby, Paul J., Cockroft, Scott L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5612056/
https://www.ncbi.nlm.nih.gov/pubmed/28970887
http://dx.doi.org/10.1039/c7sc01940h
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author Cooper, James A.
Borsley, Stefan
Lusby, Paul J.
Cockroft, Scott L.
author_facet Cooper, James A.
Borsley, Stefan
Lusby, Paul J.
Cockroft, Scott L.
author_sort Cooper, James A.
collection PubMed
description Supramolecular chirality may emerge from self-assembly processes to yield architectures that differ only in the topological arrangement of their constituent parts. Since the properties of the resulting enantiomeric assemblies are identical, purification and characterisation can be challenging. Here, we have examined the hypothesis that the intrinsic chirality of a protein nanopore can be exploited to detect supramolecular chirality. Transient blockages in the ion current flowing through a single membrane-spanning α-haemolysin nanopore were shown to discriminate between M(4)L(6) tetrahedral coordination cages of opposing chiralities. The single-molecule nature of the approach facilitated direct access to the rates of association and dissociation with the nanopore, which allowed the concentrations of the enantiomeric supramolecular assemblies to be determined in situ. Thus, we have established that a protein nanopore can be used to discriminate the chiral topologies of supramolecular assemblies, even when they are too large to fully enter the nanopore.
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spelling pubmed-56120562017-10-02 Discrimination of supramolecular chirality using a protein nanopore Cooper, James A. Borsley, Stefan Lusby, Paul J. Cockroft, Scott L. Chem Sci Chemistry Supramolecular chirality may emerge from self-assembly processes to yield architectures that differ only in the topological arrangement of their constituent parts. Since the properties of the resulting enantiomeric assemblies are identical, purification and characterisation can be challenging. Here, we have examined the hypothesis that the intrinsic chirality of a protein nanopore can be exploited to detect supramolecular chirality. Transient blockages in the ion current flowing through a single membrane-spanning α-haemolysin nanopore were shown to discriminate between M(4)L(6) tetrahedral coordination cages of opposing chiralities. The single-molecule nature of the approach facilitated direct access to the rates of association and dissociation with the nanopore, which allowed the concentrations of the enantiomeric supramolecular assemblies to be determined in situ. Thus, we have established that a protein nanopore can be used to discriminate the chiral topologies of supramolecular assemblies, even when they are too large to fully enter the nanopore. Royal Society of Chemistry 2017-07-01 2017-05-11 /pmc/articles/PMC5612056/ /pubmed/28970887 http://dx.doi.org/10.1039/c7sc01940h Text en This journal is © The Royal Society of Chemistry 2017 http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial 3.0 Unported License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Chemistry
Cooper, James A.
Borsley, Stefan
Lusby, Paul J.
Cockroft, Scott L.
Discrimination of supramolecular chirality using a protein nanopore
title Discrimination of supramolecular chirality using a protein nanopore
title_full Discrimination of supramolecular chirality using a protein nanopore
title_fullStr Discrimination of supramolecular chirality using a protein nanopore
title_full_unstemmed Discrimination of supramolecular chirality using a protein nanopore
title_short Discrimination of supramolecular chirality using a protein nanopore
title_sort discrimination of supramolecular chirality using a protein nanopore
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5612056/
https://www.ncbi.nlm.nih.gov/pubmed/28970887
http://dx.doi.org/10.1039/c7sc01940h
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