Reversible disc‐to‐vesicle transition of melittin‐DPPC complexes triggered by the phospholipid acyl chain melting

Dufourc, Érick J.; Faucon, Jean‐François; Fourche, Georges; Dufourcq, Jean; Gulik-Krzywicki, T.; Maire, Marc le

doi:10.1016/0014-5793(86)80609-3

Cited by 93 publications

(76 citation statements)

References 7 publications

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“…As indicated by the increased interaction at high salt concentration [41], binding to PC is governed by hydrophobic interaction, leading to an embedding of the hydrophobic side of the helices only, and hence a headgroup spacing effect. This 'wedge' effect, as suggested by others [3], would then induce the formation of the reported [16,19] type I (micellar) structures (Fig. 7 A2).…”

Section: Discussionsupporting

confidence: 52%

“…The vast majority of these reports were limited to the insertion of melittin into detergent micelles or phosphati- dylcholine bilayers. Our 3ap-NMR, freeze-fracture and X-ray diffraction studies however, as reported in the preceding article [1] show a remarkable difference between the structural alterations induced by melittin in the negatively charged cardiolipin system (formation of inverted non-bilayer structures) and those reported for phosphatidylcholines (formation of disc and micellar type of structures [16,19]). The hypothesis that this lipid specific structural reorganization is correlated with a different mode of insertion is addressed in this report, using fluorescence techniques.…”

Section: Introductionsupporting

confidence: 55%

“…The position of melittjn with respect to the phospholipids to which it is bound, as well as its aggregational state in this situation have been subject of several studies [2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19] and considerable debate. The vast majority of these reports were limited to the insertion of melittin into detergent micelles or phosphati- dylcholine bilayers.…”

Section: Introductionmentioning

confidence: 99%

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Lipid specific penetration of melittin into phospholipid model membranes

Batenburg

Hibbeln

Kruijff

1987

Biochimica et Biophysica Acta (BBA) - Biomembranes

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The relative depth of penetration of melittin into egg phosphatidylcholine and bovine heart cardiolipin model membranes was investigated using fluorescence spectroscopy techniques. The tryptophan intrinsic fluorescence shift suggests a more hydrophobic surrounding of this residue in cardiolipin, while the accessibility for charged and uncharged aqueous quenchers is decreased in the cardiolipin system when compared with the phosphatidylcholine-bound situation. A lipid incorporated hydrophobic, collisional quencher and a resonance energy transfer acceptor on the other hand are more effective in quenching the tryptophan fluorescence of cardiolipin bound melittin. The combination of these results is interpreted as prove of a deeper positioning of the tryptophan containing part of the peptide molecule in the cardiolipin system in comparison with the situation in phosphatidylcholine. Models that take this difference into account are presented, which try to explain the opposite effect of melittin binding to the two lipid systems with respect to supramolecular structure, as reported in the preceding article (Batenburg, A.M., Hibbeln, J.C.L., Verkleij, A

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Section: Discussionsupporting

confidence: 52%

Section: Introductionsupporting

confidence: 55%

Section: Introductionmentioning

confidence: 99%

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Lipid specific penetration of melittin into phospholipid model membranes

Batenburg

Hibbeln

Kruijff

1987

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…The second trigger is the fluid-togel phase transition. Cooling the membrane to the more ordered gel phase reduces its capacity to accommodate melittin at the interface level and, as a consequence, induces the redistribution of the peptide towards the apolar core 36,[71][72][73][74] . Third, melittin relocation from the interface can also be triggered by electrostatic repulsions at the interfacial level.…”

Section: Electrostatic Effect On Lipid Extractionmentioning

confidence: 99%

Role of the Cationic C-Terminal Segment of Melittin on Membrane Fragmentation

2016

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The widespread distribution of cationic antimicrobial peptides capable of membrane fragmentation in nature underlines their importance to living organisms. In the present work, we determined the impact of the electrostatic interactions associated with the cationic Cterminal segment of melittin, a 26-amino acid peptide from bee venom (net charge +6), on its binding to model membranes and on the resulting fragmentation. In order to detail the role played by the C-terminal charges, we prepared a melittin analogue for which the 4 cationic amino acids in positions 21 to 24 were substituted with the polar residue citrulline, providing a peptide with the same length and amphiphilicity but with a lower net charge (+2). We compared the peptide bilayer affinity and the membrane fragmentation for bilayers prepared from dipalmitoyl-sn-glycero-3-phosphocholine (DPPC)/1,2-dipalmitoyl-sn-glycero-3-phospho-L-serine (DPPS) mixtures. It is shown that neutralization of the C-terminal considerably increased melittin affinity for zwitterionic membranes. The unfavorable contribution associated with transferring the cationic C-terminal in a less polar environment was reduced, leaving the hydrophobic interactions, which drive the peptide insertion in bilayers, with limited counterbalancing interactions. The presence of negatively charged lipids (DPPS) in bilayers increased melittin binding by introducing attractive electrostatic interactions, the augmentation being, as expected, greater for native melittin than for its citrullinated analogue. The membrane fragmentation power of the peptide was shown to be controlled by electrostatic interactions and could be modulated by the charge carried by both the membrane and the lytic peptide. The analysis of the lipid composition of the extracted fragments from DPPC/DPPS bilayers revealed no lipid specificity. It is proposed that extended phase separations are more susceptible to lead to the extraction of a lipid species in a specific manner than a specific lipid-peptide affinity. The present work on the lipid extraction by melittin and citrullinated melittin with model membranes emphasizes the complex relation between the affinity, the lipid extraction/membrane fragmentation, and the lipid specificity.

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“…Bee venom melittin has recently been reported to induce reversible transitions between extended bilayers and micelles at the lipid-phase transition in bilayer membranes composed of saturated phospholipids [1][2][3][4]. In two of these studies deuterium NMR was used to characterize the interaction of melittin with bilayers composed of acyl-chain-deuterated DPPC [3] and head-groupdeuterated DMPC [4].…”

Section: Introductionmentioning

confidence: 99%

The interaction of amino‐deuteromethylated melittin with phospholipid membranes studied by deuterium NMR

1987

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Melittin, deuteromethylated on each of the four amino groups (Gly-1 Not and Lys-7, 21, and 23 Are), was prepared by reductive methylation using deuteroformaldehyde and NaBD3CN. Deuterium NMR spectra were obtained for the modified peptide (D-melittin) bound to phospholipid bilayers and erythrocyte ghosts. D-Melittin at 4 mol% (peptide:lipid) induced reversible transitions between extended bilayers and micelles at the phase-transition temperature in dimyristoylphosphatidylcholine (DMPC) bilayers. These changes in lipid morphology did not occur at 1 mol% D-melittin: DMPC and the peptide was highly motionally restricted in gel-phase lipid.

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Reversible disc‐to‐vesicle transition of melittin‐DPPC complexes triggered by the phospholipid acyl chain melting

Cited by 93 publications

References 7 publications

Lipid specific penetration of melittin into phospholipid model membranes

Lipid specific penetration of melittin into phospholipid model membranes

Role of the Cationic C-Terminal Segment of Melittin on Membrane Fragmentation

The interaction of amino‐deuteromethylated melittin with phospholipid membranes studied by deuterium NMR

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