Investigation on native vesicles containing the nicotinic acetylcholine receptor using FTIR-spectroscopy

Wolfgang B. Fischer; Gerald Steiner; Christian Kuhne; Reiner Salzer

doi:10.1016/S0022-2860(01)00508-7

Investigation on native vesicles containing the nicotinic acetylcholine receptor using FTIR-spectroscopy

Wolfgang B. Fischer^*, Gerald Steiner, Christian Kuhne, Reiner Salzer

^*Corresponding author for this work

Institute of Biophotonics

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

3 Scopus citations

Abstract

The ligand gated ion channel nicotinic acetylcholine receptor is responsible for the electrochemical signal transduction in nerve cells and at the motor endplates. In the recent years the structure of the channel has emerged to a resolution of 4.6 Å [J. Mol. Biol. 288 (1999) 765]. We have used ATR-FTIR and SEIRA spectroscopy to investigate the extramembraneous structure of the receptor. The adsorption of nicotinic acetylcholine receptor rich vesicles on the surface of Ag-cluster leads to the detection of high content of helical structure in the extra membranous parts of the receptor. Spectra indicate a β-sheet structure perpendicular to the crystal plane.

Original language	English
Pages (from-to)	153-158
Number of pages	6
Journal	Journal of Molecular Structure
Volume	570
Issue number	1-3
DOIs	https://doi.org/10.1016/S0022-2860(01)00508-7
State	Published - 1 Aug 2001

Keywords

FTIR-spectroscopy
Ion channel
nAChR
SEIRA spectroscopy

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10.1016/S0022-2860(01)00508-7

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@article{4376a6209382453484542178e3cccf96,

title = "Investigation on native vesicles containing the nicotinic acetylcholine receptor using FTIR-spectroscopy",

abstract = "The ligand gated ion channel nicotinic acetylcholine receptor is responsible for the electrochemical signal transduction in nerve cells and at the motor endplates. In the recent years the structure of the channel has emerged to a resolution of 4.6 {\AA} [J. Mol. Biol. 288 (1999) 765]. We have used ATR-FTIR and SEIRA spectroscopy to investigate the extramembraneous structure of the receptor. The adsorption of nicotinic acetylcholine receptor rich vesicles on the surface of Ag-cluster leads to the detection of high content of helical structure in the extra membranous parts of the receptor. Spectra indicate a β-sheet structure perpendicular to the crystal plane.",

keywords = "FTIR-spectroscopy, Ion channel, nAChR, SEIRA spectroscopy",

author = "Fischer, {Wolfgang B.} and Gerald Steiner and Christian Kuhne and Reiner Salzer",

note = "Funding Information: The author wants to thank A. Maelicke und A. Schrattenholz (University of Mainz) for providing the nAChR rich vesicle suspensions. Thanks also to Dr. G. B{\"o}hme (Sentronic GmbH) for preparing the Ag coated Ge crystals for recording the IR spectra. This work was supported by the Bundesministerium f{\"u}r Bildung und Forschung.",

year = "2001",

month = aug,

day = "1",

doi = "10.1016/S0022-2860(01)00508-7",

language = "English",

volume = "570",

pages = "153--158",

journal = "Journal of Molecular Structure",

issn = "0022-2860",

publisher = "Elsevier B.V.",

number = "1-3",

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TY - JOUR

T1 - Investigation on native vesicles containing the nicotinic acetylcholine receptor using FTIR-spectroscopy

AU - Fischer, Wolfgang B.

AU - Steiner, Gerald

AU - Kuhne, Christian

AU - Salzer, Reiner

N1 - Funding Information: The author wants to thank A. Maelicke und A. Schrattenholz (University of Mainz) for providing the nAChR rich vesicle suspensions. Thanks also to Dr. G. Böhme (Sentronic GmbH) for preparing the Ag coated Ge crystals for recording the IR spectra. This work was supported by the Bundesministerium für Bildung und Forschung.

PY - 2001/8/1

Y1 - 2001/8/1

N2 - The ligand gated ion channel nicotinic acetylcholine receptor is responsible for the electrochemical signal transduction in nerve cells and at the motor endplates. In the recent years the structure of the channel has emerged to a resolution of 4.6 Å [J. Mol. Biol. 288 (1999) 765]. We have used ATR-FTIR and SEIRA spectroscopy to investigate the extramembraneous structure of the receptor. The adsorption of nicotinic acetylcholine receptor rich vesicles on the surface of Ag-cluster leads to the detection of high content of helical structure in the extra membranous parts of the receptor. Spectra indicate a β-sheet structure perpendicular to the crystal plane.

AB - The ligand gated ion channel nicotinic acetylcholine receptor is responsible for the electrochemical signal transduction in nerve cells and at the motor endplates. In the recent years the structure of the channel has emerged to a resolution of 4.6 Å [J. Mol. Biol. 288 (1999) 765]. We have used ATR-FTIR and SEIRA spectroscopy to investigate the extramembraneous structure of the receptor. The adsorption of nicotinic acetylcholine receptor rich vesicles on the surface of Ag-cluster leads to the detection of high content of helical structure in the extra membranous parts of the receptor. Spectra indicate a β-sheet structure perpendicular to the crystal plane.

KW - FTIR-spectroscopy

KW - Ion channel

KW - nAChR

KW - SEIRA spectroscopy

UR - http://www.scopus.com/inward/record.url?scp=0035424492&partnerID=8YFLogxK

U2 - 10.1016/S0022-2860(01)00508-7

DO - 10.1016/S0022-2860(01)00508-7

M3 - Article

AN - SCOPUS:0035424492

SN - 0022-2860

VL - 570

SP - 153

EP - 158

JO - Journal of Molecular Structure

JF - Journal of Molecular Structure

IS - 1-3

ER -

Investigation on native vesicles containing the nicotinic acetylcholine receptor using FTIR-spectroscopy

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Keywords

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