Stochastic sensing of Angiotensin II with lysenin channels

Abstract The ability of pore-forming proteins to interact with various analytes has found vast applicability in single molecule sensing and characterization. In spite of their abundance in organisms from all kingdoms of life, only a few pore-forming proteins have been successfully reconstituted in a...

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Autores principales:	Nisha Shrestha, Sheenah L. Bryant, Christopher Thomas, Devon Richtsmeier, Xinzhu Pu, Juliette Tinker, Daniel Fologea
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5b75edd8d9644309bf79188984136256
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spelling	oai:doaj.org-article:5b75edd8d9644309bf791889841362562021-12-02T12:32:18ZStochastic sensing of Angiotensin II with lysenin channels10.1038/s41598-017-02438-02045-2322https://doaj.org/article/5b75edd8d9644309bf791889841362562017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02438-0https://doaj.org/toc/2045-2322Abstract The ability of pore-forming proteins to interact with various analytes has found vast applicability in single molecule sensing and characterization. In spite of their abundance in organisms from all kingdoms of life, only a few pore-forming proteins have been successfully reconstituted in artificial membrane systems for sensing purposes. Lysenin, a pore-forming toxin extracted from the earthworm E. fetida, inserts large conductance nanopores in lipid membranes containing sphingomyelin. Here we show that single lysenin channels may function as stochastic nanosensors by allowing the short cationic peptide angiotensin II to be electrophoretically driven through the conducting pathway. Long-term translocation experiments performed using large populations of lysenin channels allowed unequivocal identification of the unmodified analyte by Liquid Chromatography-Mass Spectrometry. However, application of reverse voltages or irreversible blockage of the macroscopic conductance of lysenin channels by chitosan addition prevented analyte translocation. This investigation demonstrates that lysenin channels have the potential to function as nano-sensing devices capable of single peptide molecule identification and characterization, which may be further extended to other macromolecular analytes.Nisha ShresthaSheenah L. BryantChristopher ThomasDevon RichtsmeierXinzhu PuJuliette TinkerDaniel FologeaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nisha Shrestha Sheenah L. Bryant Christopher Thomas Devon Richtsmeier Xinzhu Pu Juliette Tinker Daniel Fologea Stochastic sensing of Angiotensin II with lysenin channels
description	Abstract The ability of pore-forming proteins to interact with various analytes has found vast applicability in single molecule sensing and characterization. In spite of their abundance in organisms from all kingdoms of life, only a few pore-forming proteins have been successfully reconstituted in artificial membrane systems for sensing purposes. Lysenin, a pore-forming toxin extracted from the earthworm E. fetida, inserts large conductance nanopores in lipid membranes containing sphingomyelin. Here we show that single lysenin channels may function as stochastic nanosensors by allowing the short cationic peptide angiotensin II to be electrophoretically driven through the conducting pathway. Long-term translocation experiments performed using large populations of lysenin channels allowed unequivocal identification of the unmodified analyte by Liquid Chromatography-Mass Spectrometry. However, application of reverse voltages or irreversible blockage of the macroscopic conductance of lysenin channels by chitosan addition prevented analyte translocation. This investigation demonstrates that lysenin channels have the potential to function as nano-sensing devices capable of single peptide molecule identification and characterization, which may be further extended to other macromolecular analytes.
format	article
author	Nisha Shrestha Sheenah L. Bryant Christopher Thomas Devon Richtsmeier Xinzhu Pu Juliette Tinker Daniel Fologea
author_facet	Nisha Shrestha Sheenah L. Bryant Christopher Thomas Devon Richtsmeier Xinzhu Pu Juliette Tinker Daniel Fologea
author_sort	Nisha Shrestha
title	Stochastic sensing of Angiotensin II with lysenin channels
title_short	Stochastic sensing of Angiotensin II with lysenin channels
title_full	Stochastic sensing of Angiotensin II with lysenin channels
title_fullStr	Stochastic sensing of Angiotensin II with lysenin channels
title_full_unstemmed	Stochastic sensing of Angiotensin II with lysenin channels
title_sort	stochastic sensing of angiotensin ii with lysenin channels
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/5b75edd8d9644309bf79188984136256
work_keys_str_mv	AT nishashrestha stochasticsensingofangiotensiniiwithlyseninchannels AT sheenahlbryant stochasticsensingofangiotensiniiwithlyseninchannels AT christopherthomas stochasticsensingofangiotensiniiwithlyseninchannels AT devonrichtsmeier stochasticsensingofangiotensiniiwithlyseninchannels AT xinzhupu stochasticsensingofangiotensiniiwithlyseninchannels AT juliettetinker stochasticsensingofangiotensiniiwithlyseninchannels AT danielfologea stochasticsensingofangiotensiniiwithlyseninchannels
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Stochastic sensing of Angiotensin II with lysenin channels

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