Lipid-protein interactions in human plasma LDL evidenced by magnetic resonance.

Abstract:

:Low density lipoprotein (LDL) particles exhibit extremely complex three-dimensional structural organization which is still not understood at the molecular level. The aim of this study was to provide the experimental evidence of a direct non-covalent interaction of the protein part with the lipid matrix. The approach was based on the combination of (1)H NMR (600 MHz) spectroscopy with thiol-specific spin labeling of the protein (apoB). It is shown that the spectral peaks assigned to the methyl head groups of phosphatidylcholine and sphingomyelin in the (1)H spectra of LDL exhibit line broadening when otherwise free thiol groups of apoB are covalently modified by methanethiosulfonate spin label. The effect is similar in the presence of water soluble paramagnetic compound. These results indicate that fragments of apoB, which are part of the receptor binding region, are directly in contact with the solvated phospholipid head groups of the lipid matrix.

journal_name

Chem Phys Lipids

authors

Kveder M,Marinić Z,Krisko A,Vikić-Topić D,Pifat G

doi

10.1016/j.chemphyslip.2006.02.014

subject

Has Abstract

pub_date

2006-06-01 00:00:00

pages

225-9

issue

1-2

eissn

0009-3084

issn

1873-2941

pii

S0009-3084(06)00039-9

journal_volume

141

pub_type

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