Journal article

Interfacial properties of the M1 segment of the nicotinic acetylcholine receptor

EE Ambroggio, MA Villarreal, GG Montich, DTS Rijkers, MRR De Planque, F Separovic, GD Fidelio

Biophysical Chemistry | ELSEVIER | Published : 2006

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, respe..

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University of Melbourne Researchers