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Interfacial properties of the M1 segment of the nicotinic acetylcholine receptor

Interfacial properties of the M1 segment of the nicotinic acetylcholine receptor
Interfacial properties of the M1 segment of the nicotinic acetylcholine receptor
We have studied the thermodynamic, surface, and structural properties of αM1 transmembrane sequence of the nicotinic acetylcholine receptor (nAChR) by using Langmuir monolayer, FT-IR spectroscopy and molecular dynamics simulation techniques in membrane-mimicking environments. M1 spontaneously incorporates into a lipid-free air–water interface, showing a favourable adsorption free energy of - 7.2 kcal/mol. A cross-sectional molecular area of 210 Å2/molecule, a surface potential of 4.2 fV/molecule and a high stability of the film were deducted from pure M1 monolayers. FT-IR experiments and molecular dynamics simulations in membrane-mimicking environments (sodium-dodecyl-sulfate and CCl4, respectively) indicate coexistence between helical and non-helical structures. Furthermore, mixed peptide–lipid monolayers and monolayer penetration experiments were performed in order to study the peptide–lipid interaction. Mixed with condensed lipids (dipalmitoyl-phosphocholine, and dipalmitoyl-phosphoglycerol), M1 shows immiscible/miscible behaviour at low/high peptide concentration, respectively. Conversely, a complete miscible peptide–lipid interface is observed with liquid-expanded lipids (palmitoyl-oleoyl-phosphocholine, and palmitoyl-oleoyl-phosphoglycerol). Peptide penetration experiments demonstrate that the M1 peptide preferentially interacts with zwitterionic phosphocholine interfaces.
Peptide monolayer, Peptide–lipid interaction, Peptide–lipid mixed monolayers, Nicotinic acetylcholine receptor, Gibbs adsorption free energy, Molecular dynamics simulation, Peptide secondary structure, Distorted helix, Fourier-transform infrared spectroscopy, Transmembrane ?M1 peptide
0301-4622
171-176
Ambroggio, E.E.
1294765b-bf85-421c-8e7d-accc3bbe4592
Villarreal, M.A.
66cb05bb-d80b-41ff-9e8d-12c736dcd96a
Montich, G.G.
9a089552-be9c-43cd-a589-fee73c0ba233
Rijkers, D.T.S.
5efc43b1-565e-4643-ac87-f379e4787a45
de Planque, M.R.R.
a1d33d13-f516-44fb-8d2c-c51d18bc21ba
Separovic, F.
1ca03f7a-0a45-465f-a683-33928d272fcd
Fidelio, G.D.
7a6669bd-cb4b-443f-9d8b-d6b8dbd209e7
Ambroggio, E.E.
1294765b-bf85-421c-8e7d-accc3bbe4592
Villarreal, M.A.
66cb05bb-d80b-41ff-9e8d-12c736dcd96a
Montich, G.G.
9a089552-be9c-43cd-a589-fee73c0ba233
Rijkers, D.T.S.
5efc43b1-565e-4643-ac87-f379e4787a45
de Planque, M.R.R.
a1d33d13-f516-44fb-8d2c-c51d18bc21ba
Separovic, F.
1ca03f7a-0a45-465f-a683-33928d272fcd
Fidelio, G.D.
7a6669bd-cb4b-443f-9d8b-d6b8dbd209e7

Ambroggio, E.E., Villarreal, M.A., Montich, G.G., Rijkers, D.T.S., de Planque, M.R.R., Separovic, F. and Fidelio, G.D. (2006) Interfacial properties of the M1 segment of the nicotinic acetylcholine receptor. Biophysical Chemistry, 121 (3), 171-176. (doi:10.1016/j.bpc.2005.12.007).

Record type: Article

Abstract

We have studied the thermodynamic, surface, and structural properties of αM1 transmembrane sequence of the nicotinic acetylcholine receptor (nAChR) by using Langmuir monolayer, FT-IR spectroscopy and molecular dynamics simulation techniques in membrane-mimicking environments. M1 spontaneously incorporates into a lipid-free air–water interface, showing a favourable adsorption free energy of - 7.2 kcal/mol. A cross-sectional molecular area of 210 Å2/molecule, a surface potential of 4.2 fV/molecule and a high stability of the film were deducted from pure M1 monolayers. FT-IR experiments and molecular dynamics simulations in membrane-mimicking environments (sodium-dodecyl-sulfate and CCl4, respectively) indicate coexistence between helical and non-helical structures. Furthermore, mixed peptide–lipid monolayers and monolayer penetration experiments were performed in order to study the peptide–lipid interaction. Mixed with condensed lipids (dipalmitoyl-phosphocholine, and dipalmitoyl-phosphoglycerol), M1 shows immiscible/miscible behaviour at low/high peptide concentration, respectively. Conversely, a complete miscible peptide–lipid interface is observed with liquid-expanded lipids (palmitoyl-oleoyl-phosphocholine, and palmitoyl-oleoyl-phosphoglycerol). Peptide penetration experiments demonstrate that the M1 peptide preferentially interacts with zwitterionic phosphocholine interfaces.

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More information

Published date: October 2006
Keywords: Peptide monolayer, Peptide–lipid interaction, Peptide–lipid mixed monolayers, Nicotinic acetylcholine receptor, Gibbs adsorption free energy, Molecular dynamics simulation, Peptide secondary structure, Distorted helix, Fourier-transform infrared spectroscopy, Transmembrane ?M1 peptide
Organisations: Nanoelectronics and Nanotechnology

Identifiers

Local EPrints ID: 264682
URI: http://eprints.soton.ac.uk/id/eprint/264682
ISSN: 0301-4622
PURE UUID: 3034e036-fa90-49f1-b38c-27b709988c8d
ORCID for M.R.R. de Planque: ORCID iD orcid.org/0000-0002-8787-0513

Catalogue record

Date deposited: 16 Oct 2007
Last modified: 26 Nov 2019 01:43

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