Fluid and condensed ApoA-I/phospholipid monolayers provide insights into ApoA-I membrane insertion

Autor: Bernard Desbat, Mathieu Pinot, Anne Renault, Véronique Vié, Lionel Chièze, Victor M. Bolanos-Garcia, Sylvie Beaufils
Přispěvatelé: Institut de Physique de Rennes (IPR), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS), Department of Biochemistry, University of Cambridge [UK] (CAM), Chimie et Biologie des Membranes et des Nanoobjets (CBMN), Université de Bordeaux (UB)-École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2011
Předmět:
Steric effects
Spectrophotometry
Infrared
MESH: Apolipoprotein A-I
Lipid Bilayers
Phospholipid
Peptide
Surface pressure
Microscopy
Atomic Force
01 natural sciences
MESH: Recombinant Proteins
03 medical and health sciences
chemistry.chemical_compound
Membrane Lipids
Structural Biology
0103 physical sciences
Monolayer
Humans
Spectroscopy
Molecular Biology
POPC
Phospholipids
030304 developmental biology
chemistry.chemical_classification
MESH: Microscopy
Atomic Force
MESH: Phospholipids
0303 health sciences
MESH: Humans
010304 chemical physics
Apolipoprotein A-I
MESH: Spectrophotometry
Infrared
MESH: Lipid Bilayers
technology
industry
and agriculture
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Molecular biology
Recombinant Proteins
PM-IRRAS
Crystallography
Membrane
Langmuir
chemistry
lipids (amino acids
peptides
and proteins)
MESH: Membrane Lipids
AFM
apolipoproteins
ellipsometry
Zdroj: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2011, 410 (1), pp.60-76. ⟨10.1016/j.jmb.2011.04.006⟩
Journal of Molecular Biology, 2011, 410 (1), pp.60-76. ⟨10.1016/j.jmb.2011.04.006⟩
ISSN: 1089-8638
0022-2836
DOI: 10.1016/j.jmb.2011.04.006⟩
Popis: International audience; Apolipoprotein A-I (ApoA-I) is a protein implicated in the solubilization of lipids and cholesterol from cellular membranes. The study of ApoA-I in phospholipid (PL) monolayers brings relevant information about ApoA-I/PL interactions. We investigated the influence of PL charge and acyl chain organization on the interaction with ApoA-I using dipalmitoyl-phosphatidylcholine, dioleoyl-phosphatidylcholine and dipalmitoyl-phosphatidylglycerol monolayers coupled to ellipsometric, surface pressure, atomic force microscopy and infrared (polarization modulation infrared reflection-absorption spectroscopy) measurements. We show that monolayer compressibility is the major factor controlling protein insertion into PL monolayers and show evidence of the requirement of a minimal distance between lipid headgroups for insertion to occur, Moreover, we demonstrate that ApoA-I inserts deepest at the highest compressibility of the protein monolayer and that the presence of an anionic headgroup increases the amount of protein inserted in the PL monolayer and prevents the steric constrains imposed by the spacing of the headgroup. We also defined the geometry of protein clusters into the lipid monolayer by atomic force microscopy and show evidence of the geometry dependence upon the lipid charge and the distance between headgroups. Finally, we show that ApoA-I helices have a specific orientation when associated to form clusters and that this is influenced by the character of PL charges. Taken together, our results suggest that the interaction of ApoA-I with the cellular membrane may be driven by a mechanism that resembles that of antimicrobial peptide/lipid interaction.
Databáze: OpenAIRE
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