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Interaction of avidin with spin‐labelled N ‐biotinyl phosphatidylethanolamine in a lipid membrane
Author(s) -
Swamy Musti J.,
Marsh Derek
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81531-4
Subject(s) - avidin , phosphatidylethanolamine , chemistry , biotin , phosphatidylcholine , lipid bilayer , spin label , membrane , biophysics , electron paramagnetic resonance , crystallography , peripheral membrane protein , biochemistry , membrane protein , phospholipid , integral membrane protein , nuclear magnetic resonance , biology , physics
N ‐Biotinyl phosphatidylethanolamine spin labelled at the C‐14 position of the sn ‐2 chain has been incorporated at a level of 1 mol% in bilayers of dimyristoyl phosphatidylcholine, and the effects on the chain mobility of binding avidin to the biotin lipid headgroup have been studied by electron spin resonance spectroscopy. In the fluid phase, avidin causes a large and selective restriction in the chain motion of the biotin lipids to which it is attached, without perturbing appreciably the mobility of the bulk lipid chains. This specific type of lipid‐protein interaction is different in kind from that observed both with integral and peripheral membrane proteins and may be involved in transmembrane communication on ligand binding to lipid headgroups, as well as lateral communication (at high packing densities) between proteins with covalent lipid anchors.