Structural Characterization of a Cation-Selective, Self-Assembled Peptide Pore in Planar Phospholipid Bilayers.

Deplazes, E; Hartmann, LM; Cranfield, CG; Garcia, A

Structural Characterization of a Cation-Selective, Self-Assembled Peptide Pore in Planar Phospholipid Bilayers.

Deplazes, E

Hartmann, LM Cranfield, CG Garcia, A

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Publisher:: American Chemical Society
Publication Type:: Journal Article
Citation:: Journal of Physical Chemistry Letters, 2020, 11, pp. 8152-8156
Issue Date:: 2020-09-15

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Field	Value	Language
dc.contributor.author	Deplazes, E https://orcid.org/0000-0003-2052-5536
dc.contributor.author	Hartmann, LM
dc.contributor.author	Cranfield, CG
dc.contributor.author	Garcia, A https://orcid.org/0000-0002-1159-4567
dc.date.accessioned	2020-09-30T20:07:27Z
dc.date.available	2020-09-30T20:07:27Z
dc.date.issued	2020-09-15
dc.identifier.citation	Journal of Physical Chemistry Letters, 2020, 11, pp. 8152-8156
dc.identifier.issn	1948-7185
dc.identifier.issn	1948-7185
dc.identifier.uri	http://hdl.handle.net/10453/142941
dc.description.abstract	GALA is a 30-residue amphipathic peptide that self-assembles into multimeric transmembrane pores in a pH-dependent fashion. In this study, we characterize the size, multimeric structure, and cation selectivity of GALA pores in planar phospholipid bilayers using electrical impedance spectroscopy and molecular dynamics simulations. We demonstrate that in planar bilayers GALA pores are likely formed by six peptide monomers rather than eight to 12 monomers as previously reported for lipid vesicles. We further show that in planar bilayers, GALA pores exhibit previously unreported cation selectivity. We propose that the difference between the predicted pore structures in planar bilayers and lipid vesicles exemplifies the importance of phospholipid bilayer structural properties on the aggregation of transmembrane helical structures.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	American Chemical Society
dc.relation	University of Technology Sydney
dc.relation	University of Technology Sydney
dc.relation.ispartof	Journal of Physical Chemistry Letters
dc.relation.hasversion	Accepted Manuscript version	en
dc.relation.isbasedon	http://dx.doi.org/10.1021/acs.jpclett.0c02335
dc.rights	This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Physical Chemistry Letters, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.jpclett.0c02335	en
dc.rights	info:eu-repo/semantics/embargoedAccess
dc.subject	02 Physical Sciences, 03 Chemical Sciences
dc.title	Structural Characterization of a Cation-Selective, Self-Assembled Peptide Pore in Planar Phospholipid Bilayers.
dc.type	Journal Article
utslib.citation.volume	11
utslib.location.activity	United States
utslib.for	02 Physical Sciences
utslib.for	03 Chemical Sciences
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
pubs.organisational-group	/University of Technology Sydney/Strength - IBMD - Initiative for Biomedical Devices
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/DVC (Teaching and Learning)
utslib.copyright.status	open_access	*
pubs.consider-herdc	false
utslib.copyright.embargo	2021-09-09T00:00:00+1000Z
dc.date.updated	2020-09-30T20:07:19Z
pubs.publication-status	Published
pubs.volume	11

Abstract:

GALA is a 30-residue amphipathic peptide that self-assembles into multimeric transmembrane pores in a pH-dependent fashion. In this study, we characterize the size, multimeric structure, and cation selectivity of GALA pores in planar phospholipid bilayers using electrical impedance spectroscopy and molecular dynamics simulations. We demonstrate that in planar bilayers GALA pores are likely formed by six peptide monomers rather than eight to 12 monomers as previously reported for lipid vesicles. We further show that in planar bilayers, GALA pores exhibit previously unreported cation selectivity. We propose that the difference between the predicted pore structures in planar bilayers and lipid vesicles exemplifies the importance of phospholipid bilayer structural properties on the aggregation of transmembrane helical structures.

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http://hdl.handle.net/10453/142941