2001
DOI: 10.1021/bi010949d
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Interaction of the α-Helices of Apolipophorin III with the Phospholipid Acyl Chains in Discoidal Lipoprotein Particles:  A Fluorescence Quenching Study

Abstract: Quenching of tryptophan fluorescence by nitroxide-labeled phospholipids and nitroxide-labeled fatty acids was used to investigate the lipid-binding domains of apolipophorin III. The location of the Trp residues relative to the lipid bilayer was investigated in discoidal lipoprotein particles made with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine and five different single-Trp mutants of apoLp-III. A comparison of the quenching efficiencies of phospholipids containing nitroxide groups at the polar head, and … Show more

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Cited by 13 publications
(9 citation statements)
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“…The extended conformation is directly supported by the long distances separating the centers of the pairs of helices 3-4 and 4 -5 as well as by the fact that the estimates for the separation distance between the helix pairs 1-4 and 2-4 are at the limit of the maximum distances that can be estimated by FRET, suggesting than even longer distances may be possible. The extended conformation is also compatible with recent studies indicating that in discoidal lipoproteins all helices of apoLp-III appear to interact with the phospholipid acyl chains (18). Moreover, the extended conformation is consistent with a previous report showing that a disulfide mutant tethering the helices 1 and 5 (22) is unable to interact with liposomes of phosphatidylcholine, leading to the spontaneous formation of discoidal lipoproteins.…”
Section: Conformation Of Apolp-iii In the Lipid-bound State Inferred supporting
confidence: 92%
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“…The extended conformation is directly supported by the long distances separating the centers of the pairs of helices 3-4 and 4 -5 as well as by the fact that the estimates for the separation distance between the helix pairs 1-4 and 2-4 are at the limit of the maximum distances that can be estimated by FRET, suggesting than even longer distances may be possible. The extended conformation is also compatible with recent studies indicating that in discoidal lipoproteins all helices of apoLp-III appear to interact with the phospholipid acyl chains (18). Moreover, the extended conformation is consistent with a previous report showing that a disulfide mutant tethering the helices 1 and 5 (22) is unable to interact with liposomes of phosphatidylcholine, leading to the spontaneous formation of discoidal lipoproteins.…”
Section: Conformation Of Apolp-iii In the Lipid-bound State Inferred supporting
confidence: 92%
“…Additional experimental evidence about the topology of apoLp-III in discoidal lipoproteins was recently presented in a fluorescence-quenching study. The quenching pattern of single-Trp mutants obtained with phospholipids containing quenchers at different depths was shown to be consistent with a location of apoLp-III around the periphery of the disc bilayer (18).…”
Section: Discussionsupporting
confidence: 60%
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“…Lipoprotein complexes of Lsd 2 and DMPG were obtained by the cholate dialysis method amply used to obtain lipoprotein particles with apolipoproteins [18] and recently used to obtain phospholipid-Lsd1complexes [13]. Lsd2 formed small lipoprotein complexes suitable for spectroscopic studies.…”
Section: Secondary Structure Of Lsd2 In the Lipid-free And Lipid-bounmentioning
confidence: 99%