Artículos
Título:
Interfacial properties of the M1 segment of the nicotinic acetylcholine receptor.
Autor/es:
AMBROGGIO EE, VILLARREAL MA, MONTICH GG, RIJKERS DT, DE PLANQUE MR, SEPAROVIC F, FIDELIO GD.
Revista:
BIOPHYSICAL CHEMISTRY
Referencias:
Año: 2006 vol. 121 p. 171 - 171
Resumen:
e 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-phosphocholine, an