Structural changes in single membranes in response to an applied transmembrane electric potential revealed by time-resolved neutron/X-ray interferometry

A. Tronin; C. H. Chen; S. Gupta; D. Worcester; V. Lauter; J. Strzalka; I. Kuzmenko; J. K. Blasie

doi:10.1016/j.chemphys.2013.01.016

Structural changes in single membranes in response to an applied transmembrane electric potential revealed by time-resolved neutron/X-ray interferometry

A. Tronin, C. H. Chen, S. Gupta, D. Worcester, V. Lauter, J. Strzalka, I. Kuzmenko, J. K. Blasie

Research output: Contribution to journal › Article › peer-review

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Abstract

The profile structure of a hybrid lipid bilayer, tethered to the surface of an inorganic substrate and fully hydrated with a bulk aqueous medium in an electrochemical cell, was investigated as a function of the applied transbilayer electric potential via time-resolved neutron reflectivity, enhanced by interferometry. Significant, and fully reversible structural changes were observed in the distal half (with respect to the substrate surface) of the hybrid bilayer comprised of a zwitterionic phospholipid in response to a +100 mV potential with respect to 0 mV. These arise presumably due to reorientation of the electric dipole present in the polar headgroup of the phospholipid and its resulting effect on the thickness of the phospholipid's hydrocarbon chain layer within the hybrid bilayer's profile structure. The profile structure of the voltage-sensor domain from a voltage-gated ion channel protein within a phospholipid bilayer membrane, tethered to the surface of an inorganic substrate and fully hydrated with a bulk aqueous medium in an electrochemical cell, was also investigated as a function of the applied transmembrane electric potential via time-resolved X-ray reflectivity, enhanced by interferometry. Significant, fully-reversible, and different structural changes in the protein were detected in response to ±100 mV potentials with respect to 0 mV. The approach employed is that typical of transient spectroscopy, shown here to be applicable to both neutron and X-ray reflectivity of thin films.

Original language	English
Pages (from-to)	283-289
Number of pages	7
Journal	Chemical Physics
Volume	422
DOIs	https://doi.org/10.1016/j.chemphys.2013.01.016
State	Published - 2013
Externally published	Yes

Funding

We acknowledge C. Liu (X-ray Science Division, Argonne National Laboratory) for fabrication of the inorganic multilayer substrates, W. Pennie (Research Instrumentation Services, University of Pennsylvania) for fabrication of the electrochemical cells, R. Goyette & H. Ambaye (Spallation Neutron Source, Oak Ridge National Laboratory) for assistance with the reflectometer and data acquisition, and G. DasGupta & S.H. White (Medical School, University of California Irvine) for providing the VSD protein, and funding via the National Institutes of Health grant P01 GM86685. The Spallation Neutron Source at Oak Ridge National Laboratory is a user facility supported by the U.S. Department of Energy, Office of Basic Energy Sciences. The Advanced Photon Source at Argonne National Laboratory is also a user facility supported by the U.S. Department of Energy, Office of Basic Energy Sciences, under Contract DE-AC02-06CH11357.

Funders	Funder number
Office of Basic Energy Sciences
U.S. Department of Energy
Argonne National Laboratory	DE-AC02-06CH11357

Keywords

Electric potential
Electrochemical cell
Hybrid bilayer
Multilayer substrate
Reconstituted membrane
Time-resolved
Time-resolved neutron interferometry
Voltage-sensor domain protein
X-ray interferometry

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10.1016/j.chemphys.2013.01.016

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title = "Structural changes in single membranes in response to an applied transmembrane electric potential revealed by time-resolved neutron/X-ray interferometry",

abstract = "The profile structure of a hybrid lipid bilayer, tethered to the surface of an inorganic substrate and fully hydrated with a bulk aqueous medium in an electrochemical cell, was investigated as a function of the applied transbilayer electric potential via time-resolved neutron reflectivity, enhanced by interferometry. Significant, and fully reversible structural changes were observed in the distal half (with respect to the substrate surface) of the hybrid bilayer comprised of a zwitterionic phospholipid in response to a +100 mV potential with respect to 0 mV. These arise presumably due to reorientation of the electric dipole present in the polar headgroup of the phospholipid and its resulting effect on the thickness of the phospholipid's hydrocarbon chain layer within the hybrid bilayer's profile structure. The profile structure of the voltage-sensor domain from a voltage-gated ion channel protein within a phospholipid bilayer membrane, tethered to the surface of an inorganic substrate and fully hydrated with a bulk aqueous medium in an electrochemical cell, was also investigated as a function of the applied transmembrane electric potential via time-resolved X-ray reflectivity, enhanced by interferometry. Significant, fully-reversible, and different structural changes in the protein were detected in response to ±100 mV potentials with respect to 0 mV. The approach employed is that typical of transient spectroscopy, shown here to be applicable to both neutron and X-ray reflectivity of thin films.",

keywords = "Electric potential, Electrochemical cell, Hybrid bilayer, Multilayer substrate, Reconstituted membrane, Time-resolved, Time-resolved neutron interferometry, Voltage-sensor domain protein, X-ray interferometry",

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AU - Tronin, A.

AU - Chen, C. H.

AU - Gupta, S.

AU - Worcester, D.

AU - Lauter, V.

AU - Strzalka, J.

AU - Kuzmenko, I.

AU - Blasie, J. K.

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N2 - The profile structure of a hybrid lipid bilayer, tethered to the surface of an inorganic substrate and fully hydrated with a bulk aqueous medium in an electrochemical cell, was investigated as a function of the applied transbilayer electric potential via time-resolved neutron reflectivity, enhanced by interferometry. Significant, and fully reversible structural changes were observed in the distal half (with respect to the substrate surface) of the hybrid bilayer comprised of a zwitterionic phospholipid in response to a +100 mV potential with respect to 0 mV. These arise presumably due to reorientation of the electric dipole present in the polar headgroup of the phospholipid and its resulting effect on the thickness of the phospholipid's hydrocarbon chain layer within the hybrid bilayer's profile structure. The profile structure of the voltage-sensor domain from a voltage-gated ion channel protein within a phospholipid bilayer membrane, tethered to the surface of an inorganic substrate and fully hydrated with a bulk aqueous medium in an electrochemical cell, was also investigated as a function of the applied transmembrane electric potential via time-resolved X-ray reflectivity, enhanced by interferometry. Significant, fully-reversible, and different structural changes in the protein were detected in response to ±100 mV potentials with respect to 0 mV. The approach employed is that typical of transient spectroscopy, shown here to be applicable to both neutron and X-ray reflectivity of thin films.

AB - The profile structure of a hybrid lipid bilayer, tethered to the surface of an inorganic substrate and fully hydrated with a bulk aqueous medium in an electrochemical cell, was investigated as a function of the applied transbilayer electric potential via time-resolved neutron reflectivity, enhanced by interferometry. Significant, and fully reversible structural changes were observed in the distal half (with respect to the substrate surface) of the hybrid bilayer comprised of a zwitterionic phospholipid in response to a +100 mV potential with respect to 0 mV. These arise presumably due to reorientation of the electric dipole present in the polar headgroup of the phospholipid and its resulting effect on the thickness of the phospholipid's hydrocarbon chain layer within the hybrid bilayer's profile structure. The profile structure of the voltage-sensor domain from a voltage-gated ion channel protein within a phospholipid bilayer membrane, tethered to the surface of an inorganic substrate and fully hydrated with a bulk aqueous medium in an electrochemical cell, was also investigated as a function of the applied transmembrane electric potential via time-resolved X-ray reflectivity, enhanced by interferometry. Significant, fully-reversible, and different structural changes in the protein were detected in response to ±100 mV potentials with respect to 0 mV. The approach employed is that typical of transient spectroscopy, shown here to be applicable to both neutron and X-ray reflectivity of thin films.

KW - Electric potential

KW - Electrochemical cell

KW - Hybrid bilayer

KW - Multilayer substrate

KW - Reconstituted membrane

KW - Time-resolved

KW - Time-resolved neutron interferometry

KW - Voltage-sensor domain protein

KW - X-ray interferometry

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VL - 422

SP - 283

EP - 289

JO - Chemical Physics

JF - Chemical Physics

ER -

Structural changes in single membranes in response to an applied transmembrane electric potential revealed by time-resolved neutron/X-ray interferometry

Abstract

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Keywords

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