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Monolayers of a model anesthetic-binding membrane protein: formation, characterization, and halothane-binding affinity.

Abstract：

:hbAP0 is a model membrane protein designed to possess an anesthetic-binding cavity in its hydrophilic domain and a cation channel in its hydrophobic domain. Grazing incidence x-ray diffraction shows that hbAP0 forms four-helix bundles that are vectorially oriented within Langmuir monolayers at the air-water interface. Single monolayers of hbAP0 on alkylated solid substrates would provide an optimal system for detailed structural and dynamical studies of anesthetic-peptide interaction via x-ray and neutron scattering and polarized spectroscopic techniques. Langmuir-Blodgett and Langmuir-Schaeffer deposition and self-assembly techniques were used to form single monolayer films of the vectorially oriented peptide hbAP0 via both chemisorption and physisorption onto suitably alkylated solid substrates. The films were characterized by ultraviolet absorption, ellipsometry, circular dichroism, and polarized Fourier transform infrared spectroscopy. The alpha-helical secondary structure of the peptide was retained in the films. Under certain conditions, the average orientation of the helical axis was inclined relative to the plane of the substrate, approaching perpendicular in some cases. The halothane-binding affinity of the vectorially oriented hbAP0 peptide in the single monolayers, with the volatile anesthetic introduced into the moist vapor environment of the monolayer, was found to be similar to that for the detergent-solubilized peptide.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Churbanova IY,Tronin A,Strzalka J,Gog T,Kuzmenko I,Johansson JS,Blasie JK

doi

10.1529/biophysj.105.072348

subject

Has Abstract

pub_date

2006-05-01 00:00:00

pages

3255-66

issue

9

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(06)72508-5

journal_volume

90

pub_type

杂志文章

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