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Issue 7, 2017
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Discrimination of supramolecular chirality using a protein nanopore

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Abstract

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 M4L6 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.

Graphical abstract: Discrimination of supramolecular chirality using a protein nanopore

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Supplementary files

Article information


Submitted
01 May 2017
Accepted
04 May 2017
First published
11 May 2017

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2017,8, 5005-5009
Article type
Edge Article

Discrimination of supramolecular chirality using a protein nanopore

J. A. Cooper, S. Borsley, P. J. Lusby and S. L. Cockroft, Chem. Sci., 2017, 8, 5005
DOI: 10.1039/C7SC01940H

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