FIDELIO GERARDO DANIEL
Artículos
Título:
Interfacial properties of the M1 segment of the nicotinic acetylcholine receptor.
Autor/es:
AMBROGGIO E.E,,; VILLARREAL M.A.,; MONTICH G.G.,; RIJKERS D.T,; DE PLANQUE MR.,; SEPAROVIC F,; FIDELIO G.D.
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Año: 2006 vol. 121 p. 171 - 171
Resumen:
p class="abstract">We have studied the thermodynamic, surface, and structural properties of alphaM1 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 A(2)/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 CCl(4), 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-phosphocholi