Phospholipid complexation and association with apolipoprotein C-II: insights from mass spectrometry.

Abstract:

:The interactions between phospholipid molecules in suspensions have been studied by using mass spectrometry. Electrospray mass spectra of homogeneous preparations formed from three different phospholipid molecules demonstrate that under certain conditions interactions between 90 and 100 lipid molecules can be preserved. In the presence of apolipoprotein C-II, a phospholipid binding protein, a series of lipid molecules and the protein were observed in complexes. The specificity of binding was demonstrated by proteolysis; the resulting mass spectra reveal lipid-bound peptides that encompass the proposed lipid-binding domain. The mass spectra of heterogeneous suspensions and their complexes with apolipoprotein C-II demonstrate that the protein binds simultaneously to two different phospholipids. Moreover, when apolipoprotein C-II is added to lipid suspensions formed with local concentrations of the same lipid molecule, the protein is capable of remodeling the distribution to form one that is closer to a statistical arrangement. These observations demonstrate a capacity for apolipoprotein C-II to change the topology of the phospholipid surface. More generally, these results highlight the fact that mass spectrometry can be used to probe lipid interactions in both homogeneous and heterogeneous suspensions and demonstrate reorganization of the distribution of lipids upon surface binding of apolipoprotein C-II.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Hanson CL,Ilag LL,Malo J,Hatters DM,Howlett GJ,Robinson CV

doi

10.1016/S0006-3495(03)74795-X

subject

Has Abstract

pub_date

2003-12-01 00:00:00

pages

3802-12

issue

6

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(03)74795-X

journal_volume

85

pub_type

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