A light-actuated nanovalve derived from a channel protein

A Kocer; M Walko; W Meijberg; Bernard Feringa

doi:10.1126/science.1114760

A light-actuated nanovalve derived from a channel protein

A Kocer, M Walko, W Meijberg, Bernard Feringa

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

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Abstract

Toward the realization of nanoscale device control, we report a molecular valve embedded in a membrane that can be opened by illumination with long-wavelength ultraviolet (366 nanometers) tight and then resealed by visible irradiation. The valve consists of a channel protein, the mechanosensitive channel of large conductance (MscL) from Escherichia coli, modified by attachment of synthetic compounds that undergo tight-induced charge separation to reversibly open and close a 3-nanometer pore. The system is compatible with a classical encapsulation system, the liposome, and external photochemical control over transport through the channel is achieved.

Original language	English
Pages (from-to)	755-758
Number of pages	4
Journal	Science
Volume	309
Issue number	5735
DOIs	https://doi.org/10.1126/science.1114760
Publication status	Published - 29-Jul-2005

Keywords

MECHANOSENSITIVE ION-CHANNEL
ESCHERICHIA-COLI-CELLS
OSMOTIC DOWNSHOCK
LARGE-CONDUCTANCE
GATING MECHANISM
SINGLE RESIDUE
MSCL
ACTIVATION
MUTATIONS

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Cite this

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title = "A light-actuated nanovalve derived from a channel protein",

abstract = "Toward the realization of nanoscale device control, we report a molecular valve embedded in a membrane that can be opened by illumination with long-wavelength ultraviolet (366 nanometers) tight and then resealed by visible irradiation. The valve consists of a channel protein, the mechanosensitive channel of large conductance (MscL) from Escherichia coli, modified by attachment of synthetic compounds that undergo tight-induced charge separation to reversibly open and close a 3-nanometer pore. The system is compatible with a classical encapsulation system, the liposome, and external photochemical control over transport through the channel is achieved.",

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author = "A Kocer and M Walko and W Meijberg and Bernard Feringa",

note = "Relation: http://www.rug.nl/scheikunde/ date_submitted:2005 Rights: University of Groningen. Stratingh Institute",

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T1 - A light-actuated nanovalve derived from a channel protein

AU - Kocer, A

AU - Walko, M

AU - Meijberg, W

AU - Feringa, Bernard

N1 - Relation: http://www.rug.nl/scheikunde/ date_submitted:2005 Rights: University of Groningen. Stratingh Institute

PY - 2005/7/29

Y1 - 2005/7/29

N2 - Toward the realization of nanoscale device control, we report a molecular valve embedded in a membrane that can be opened by illumination with long-wavelength ultraviolet (366 nanometers) tight and then resealed by visible irradiation. The valve consists of a channel protein, the mechanosensitive channel of large conductance (MscL) from Escherichia coli, modified by attachment of synthetic compounds that undergo tight-induced charge separation to reversibly open and close a 3-nanometer pore. The system is compatible with a classical encapsulation system, the liposome, and external photochemical control over transport through the channel is achieved.

AB - Toward the realization of nanoscale device control, we report a molecular valve embedded in a membrane that can be opened by illumination with long-wavelength ultraviolet (366 nanometers) tight and then resealed by visible irradiation. The valve consists of a channel protein, the mechanosensitive channel of large conductance (MscL) from Escherichia coli, modified by attachment of synthetic compounds that undergo tight-induced charge separation to reversibly open and close a 3-nanometer pore. The system is compatible with a classical encapsulation system, the liposome, and external photochemical control over transport through the channel is achieved.

KW - MECHANOSENSITIVE ION-CHANNEL

KW - ESCHERICHIA-COLI-CELLS

KW - OSMOTIC DOWNSHOCK

KW - LARGE-CONDUCTANCE

KW - GATING MECHANISM

KW - SINGLE RESIDUE

KW - MSCL

KW - ACTIVATION

KW - MUTATIONS

U2 - 10.1126/science.1114760

DO - 10.1126/science.1114760

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VL - 309

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EP - 758

JO - Science

JF - Science

IS - 5735

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