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Biophys J, October 2000, p. 2024-2032, Vol. 79, No. 4
*Department of Physics and Physical Oceanography, Memorial
University of Newfoundland, St. John's, Newfoundland A1B 3X7, Canada;
and Department of Biochemistry, University of Western
Ontario, London, Ontario N6A 5C1, Canada
A peptide containing the transmembrane domain of the
human EGF receptor was studied in fluid lipid bilayers for insight into receptor tyrosine kinase lateral associations in cell membranes. The
peptide comprised the 23-amino acid hydrophobic segment thought to span
the membrane (Ile622 to Met644 of the EGF
receptor), plus the first 10 amino acids of the receptor's cytoplasmic
domain (Arg645 to Thr654). Probes for
solid-state NMR spectroscopy were incorporated by deuteration of the
methyl side chains of alanine at positions 623 and 637. 2H-NMR spectra were recorded from 25 to 65°C in membranes
composed of 1-palmitoyl-2-oleoyl phosphatidylcholine, with and without 33% cholesterol, and relaxation times were measured. Peptide
concentration ranged from 0.5 to 10 mol %. The peptide behaved as
predominant monomers undergoing rapid symmetric rotational diffusion;
however, there was evidence of reversible side-to-side interaction
among the hydrophobic transmembrane domains, particularly at
physiological temperatures and in the presence of natural
concentrations of cholesterol. The results of these experiments in
fluid membranes are consistent with the existence of lipid-protein
interactions that would predispose to receptor microdomain formation in
membranes of higher animal cells.
Biophys J, October 2000, p. 2024-2032, Vol. 79, No. 4
© 2000 by the Biophysical Society 0006-3495/00/10/2024/09 $2.00
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