Calcium Ion Binding at the Lipid-Water Interface Alters the Ion Permeability of Phospholipid Bilayers.

Deplazes, E; Tafalla, BD; Murphy, C; White, J; Cranfield, CG; Garcia, A

Calcium Ion Binding at the Lipid-Water Interface Alters the Ion Permeability of Phospholipid Bilayers.

Deplazes, E

Tafalla, BD Murphy, C White, J Cranfield, CG Garcia, A

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Publisher:: American Chemical Society (ACS)
Publication Type:: Journal Article
Citation:: Langmuir, 2021, 37, (48), pp. 14026-14033
Issue Date:: 2021-12-07

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Field	Value	Language
dc.contributor.author	Deplazes, E https://orcid.org/0000-0003-2052-5536
dc.contributor.author	Tafalla, BD
dc.contributor.author	Murphy, C
dc.contributor.author	White, J
dc.contributor.author	Cranfield, CG
dc.contributor.author	Garcia, A https://orcid.org/0000-0002-1159-4567
dc.date.accessioned	2022-01-12T05:38:38Z
dc.date.available	2022-01-12T05:38:38Z
dc.date.issued	2021-12-07
dc.identifier.citation	Langmuir, 2021, 37, (48), pp. 14026-14033
dc.identifier.issn	0743-7463
dc.identifier.issn	1520-5827
dc.identifier.uri	http://hdl.handle.net/10453/152982
dc.description.abstract	Calcium ions (Ca2+) play a fundamental role in membrane-associated physiological processes. Ca2+ can also significantly modulate the physicochemical properties of phospholipid bilayers, but whether this occurs at physiologically relevant concentrations is difficult to determine because of the uncertainty in the reported affinity of Ca2+ for phospholipid bilayers. In this article, we determine the apparent affinity of Ca2+ for zwitterionic phospholipid bilayers using tethered bilayer lipid membranes (tBLMs) used in conjunction with swept-frequency electrical impedance spectroscopy (EIS). We report that Ca2+ binds to phospholipid bilayers at physiologically relevant concentrations and modulates membrane permeability. We present direct experimental evidence that this effect is governed by specific interactions with select lipid headgroup moieties, which is supported by data from molecular dynamics (MD) simulations. This is the first reported use of tBLM/EIS to estimate cation-membrane affinity. Combined with MD simulations, this technique provides a novel methodology to elucidate the molecular details of cation-membrane interactions at the water-phospholipid interface.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	American Chemical Society (ACS)
dc.relation.ispartof	Langmuir
dc.relation.isbasedon	10.1021/acs.langmuir.1c02016
dc.rights	info:eu-repo/semantics/closedAccess
dc.subject.classification	Chemical Physics
dc.title	Calcium Ion Binding at the Lipid-Water Interface Alters the Ion Permeability of Phospholipid Bilayers.
dc.type	Journal Article
utslib.citation.volume	37
utslib.location.activity	United States
pubs.organisational-group	/University of Technology Sydney
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/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney/Strength - IBMD - Initiative for Biomedical Devices
pubs.organisational-group	/University of Technology Sydney/Centre for Health Technologies (CHT)
utslib.copyright.status	closed_access	*
dc.date.updated	2022-01-12T05:38:21Z
pubs.issue	48
pubs.publication-status	Published
pubs.volume	37
utslib.citation.issue	48

Abstract:

Calcium ions (Ca2+) play a fundamental role in membrane-associated physiological processes. Ca2+ can also significantly modulate the physicochemical properties of phospholipid bilayers, but whether this occurs at physiologically relevant concentrations is difficult to determine because of the uncertainty in the reported affinity of Ca2+ for phospholipid bilayers. In this article, we determine the apparent affinity of Ca2+ for zwitterionic phospholipid bilayers using tethered bilayer lipid membranes (tBLMs) used in conjunction with swept-frequency electrical impedance spectroscopy (EIS). We report that Ca2+ binds to phospholipid bilayers at physiologically relevant concentrations and modulates membrane permeability. We present direct experimental evidence that this effect is governed by specific interactions with select lipid headgroup moieties, which is supported by data from molecular dynamics (MD) simulations. This is the first reported use of tBLM/EIS to estimate cation-membrane affinity. Combined with MD simulations, this technique provides a novel methodology to elucidate the molecular details of cation-membrane interactions at the water-phospholipid interface.

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http://hdl.handle.net/10453/152982