References of "Chemistry and Physics of Lipids"
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See detailEffect Of The Antibiotic Azithromycin On Thermotropic Behavior Of Dopc Or Dppc Bilayers
Fa, N.; Ronkart, Sébastien ULg; Schanck, A. et al

in Chemistry and Physics of Lipids (2006), 144(1),

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See detailLipid-Destabilising Properties Of A Peptide With Structural Plasticity
Lorin, A.; Thomas, Annick ULg; Stroobant, V. et al

in Chemistry and Physics of Lipids (2006), 141(1-2), 185-96

The Chameleon peptide (Cham) is a peptide designed from two regions of the GB1 protein, one folded as an alpha-helix and the other as a beta structure. Depending on the environment, the Cham peptide ... [more ▼]

The Chameleon peptide (Cham) is a peptide designed from two regions of the GB1 protein, one folded as an alpha-helix and the other as a beta structure. Depending on the environment, the Cham peptide adopts an alpha or a beta conformation when inserted in different locations of GB1. This environment dependence is also observed for tilted peptides. These short protein fragments, able to destabilise organised system, are mainly folded in beta structure in water and in alpha helix in a hydrophobic environment, like the lipid bilayer. In this paper, we tested whether the Cham peptide can be qualified as a tilted peptide. For this, we have compared the properties of Cham peptide (hydrophobicity, destabilising properties, conformation) to those of tilted peptides. The results suggest that Cham is a tilted peptide. Our study, together the presence of tilted fragments in transconformational proteins, suggests a relationship between tilted peptides and structural lability. [less ▲]

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See detailMembrane Destabilization Induced By Beta-Amyloid Peptide 29-42: Importance Of The Amino-Terminus
Mingeot-Leclercq, Mp.; Lins, Laurence ULg; Bensliman, M. et al

in Chemistry and Physics of Lipids (2002), 120(1-2), 57-74

Increasing evidence implicates interactions between Abeta-peptides and membrane lipids in Alzheimer's disease. To gain insight into the potential role of the free amino group of the N-terminus of Abeta29 ... [more ▼]

Increasing evidence implicates interactions between Abeta-peptides and membrane lipids in Alzheimer's disease. To gain insight into the potential role of the free amino group of the N-terminus of Abeta29-42 fragment in these processes, we have investigated the ability of Abeta29-42 unprotected and Abeta29-42 N-protected to interact with negatively-charged liposomes and have calculated the interaction with membrane lipids by conformational analysis. Using vesicles mimicking the composition of neuronal membranes, we show that both peptides have a similar capacity to induce membrane fusion and permeabilization. The fusogenic effect is related to the appearance of non-bilayer structures where isotropic motions occur as shown by 31P and 2H NMR studies. The molecular modeling calculations confirm the experimental observations and suggest that lipid destabilization could be due to the ability of both peptides to adopt metastable positions in the presence of lipids. In conclusion, the presence of a free or protected (acetylated) amino group in the N-terminus of Abeta29-42 is therefore probably not crucial for destabilizing properties of the C-terminal fragment of Abeta peptides. [less ▲]

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See detailAminoglycoside Antibiotics Prevent The Formation Of Non-Bilayer Structures In Negatively-Charged Membranes. Comparative Studies Using Fusogenic (Bis(Beta-Diethylaminoethylether)Hexestrol) And Aggregating (Spermine) Agents
Vanbambeke, F.; Mingeotleclercq, Mp.; Brasseur, Robert ULg et al

in Chemistry and Physics of Lipids (1996), 79(2), 123-35

Aminoglycoside antibiotics cause aggregation but not fusion of negatively-charged liposomes at an extent proportional to their capacity to interact with acidic phospholipids (Van Bambeke et al., 1995, Eur ... [more ▼]

Aminoglycoside antibiotics cause aggregation but not fusion of negatively-charged liposomes at an extent proportional to their capacity to interact with acidic phospholipids (Van Bambeke et al., 1995, Eur. J. Pharmacol., 289, 321-333). To understand why aggregation is not followed by fusion, we have examined here the influence of two aminoglycosides with markedly different toxic potential (gentamicin > isepamicin) on lipid phase transition in negatively-charged liposomes using 31P-NMR spectroscopy, in comparison with spermine (an aggregating agent) and bis(beta-diethylaminoethylether)hexestrol or DEH (a fusogenic cationic amphiphile). Gentamicin, spermine, and, to a lesser extent, isepamicin inhibit the appearance of the isotropic signal seen upon warming of control liposomes and denoting the presence of mobile structures. This non-bilayer signal appeared most prominently when liposomes were incubated with DEH, a strong fusogenic agent. We conclude that aminoglycosides, like spermine, have the potential to prevent membrane fusion, by inhibiting the development of a critical change in membrane organization, which is associated with fusion. We suggest that this capacity could be a determinant in aminoglycoside toxicity. [less ▲]

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