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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,...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Royal Society of Chemistry
2017
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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. |
format | Online Article Text |
id | pubmed-5612056 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
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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