Open AccessInteraction of Apoprotein from Porcine High‐Density Lipoprotein with Dimyristoyl Lecithin
Author(s) -
ANDREWS Anthony L.,
ATKINSON David,
BARRATT Martin D.,
FINER Elliot G.,
HAUSER Helmut,
HENRY Robert,
LESLIE Robert B.,
OWENS Nicholas L.,
PHILLIPS Michael. C.,
ROBERTSON R. Neil
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb10335.x
Subject(s) - lecithin , chemistry , lipid bilayer , phosphatidylcholine , crystallography , bilayer , biophysics , lipid bilayer phase behavior , molecule , lipoprotein , model lipid bilayer , biochemistry , membrane , phospholipid , cholesterol , organic chemistry , biology
The detailed molecular structure of the complex formed by the apoprotein from porcine high density lipoprotein and dimyristoyl phosphatidylcholine (lecithin) has been investigated by a range of physical techniques. The complex, an oblate ellipsoid with major axis 11.0 nm and minor axis 5.5 nm (see the accompanying paper), is comprised of a section of lecithin bilayer with apoprotein at the surface. The main site of interaction between protein and lipid is in the lipid glycerophosphorylcholine group region; as with native high density lipoprotein the surface of the particle consists of a mosaic of lecithin polar groups and protein. The formation of this mosaic reduces the cooperativity of the lecithin chain motions and changes the curvature of the lipid‐water interface, as compared to a bilayer. Otherwise, there are no major changes in lecithin motions indicating that no strong binding of lipid to protein occurs. The interaction involves the intercalation of amphipathic, 60%α‐helical, apoprotein molecules among the lecithin molecules so that the protein resides at the lipid‐watet interface. The apoprotein has a high affinity for the lipid‐water interface but specific lipid‐protein interactions are not involved.