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J Biol Chem, Vol. 274, Issue 30, 20839-20846, July 23, 1999
From the Specific interactions of membrane proteins with
the membrane interfacial region potentially define protein position
with respect to the lipid environment. We investigated the proposed
roles of tryptophan and lysine side chains as "anchoring" residues
of transmembrane proteins. Model systems were employed, consisting of
phosphatidylcholine lipids and hydrophobic
Different Membrane Anchoring Positions of Tryptophan and
Lysine in Synthetic Transmembrane
-Helical Peptides
,
,, and
Department Biochemistry of Membranes, Center
for Biomembranes and Lipid Enzymology, Institute of Biomembranes,
Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands, the
¶ Department of Medicinal Chemistry, Utrecht University,
Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands, Abteilung
Spektroskopie, Max-Planck-Institut für biophysikalische
Chemie, D-37077 Göttingen, Germany, and the ** Department of
Chemistry and Biochemistry, University of Arkansas,
Fayetteville, Arkansas 72701
-helical peptides,
flanked either by tryptophans or lysines. Peptides were incorporated in
bilayers of different thickness, and effects on lipid structure were
analyzed. Induction of nonbilayer phases and also increases in bilayer
thickness were observed that could be explained by a tendency of Trp as
well as Lys residues to maintain interactions with the interfacial region. However, effects of the two peptides were remarkably different, indicating affinities of Trp and Lys for different sites at the interface. Our data support a model in which the Trp side chain has a
specific affinity for a well defined site near the lipid carbonyl
region, while the lysine side chain prefers to be located closer to the
aqueous phase, near the lipid phosphate group. The information obtained
in this study may further our understanding of the architecture of
transmembrane proteins and may prove useful for refining prediction
methods for transmembrane segments.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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