Incorporation of Melittin into phosphatidylcholine bilayers

Vogel, Horst

doi:10.1016/0014-5793(81)80545-5

Cited by 178 publications

(138 citation statements)

References 19 publications

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“…This observation shows that the local environment of the peptides can either promote or oppose the formation of secondary structure. Consistent with previous studies (Vogel, 1981 ;Beschiaschvili & Seelig, 1990), melittin displayed a significant increase in helicity upon mixing with liposomes. Even though melittin's hydrophobic moment is smaller than that for SI, its increase in CYhelicity was significantly greater, again emphasizing the balanced role that electrostatic and hydrophobic forces play in the formation of secondary structure.…”

Section: Structural Aspects Of Peptide-lipid Interactionssupporting

confidence: 92%

A molecular model for membrane fusion based on solution studies of an amphiphilic peptide from HIV gp41

et al. 1992

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The mechanism of protein-mediated membrane fusion and lysis has been investigated by solution-state studies of the effects of peptides on liposomes. A peptide (SI) corresponding to a highly amphiphilic C-terminal segment from the envelope protein (gp41) of the human immunodeficiency virus (HIV) was synthesized and tested for its ability to cause lipid membranes to fuse together (fusion) or to break open (lysis). These effects were compared to those produced by the lytic and fusogenic peptide from bee venom, melittin. Other properties studied included the changes in visible absorbance and mean particle size, and the secondary structure of peptides as judged by CD spectroscopy. Taken together, the observations suggest that protein-mediated membrane fusion is dependent not only on hydrophobic and electrostatic forces but also on the spatial arrangement of the amino acid residues to form an amphiphilic structure that promotes the mixing of the lipids between membranes. A speculative molecular model is proposed for membrane fusion by a-helical peptides, and its relationship to the forces involved in protein-membrane interactions is discussed.

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Section: Structural Aspects Of Peptide-lipid Interactionssupporting

confidence: 92%

A molecular model for membrane fusion based on solution studies of an amphiphilic peptide from HIV gp41

et al. 1992

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“…3, binding results in a 20 nm blue shift and increased intensity of the emission, both indicative of a more hydrophobic environment, most likely formed by the apolar parts of the lipids. Binding to egg-PC vesicles effects a shift of only 16 to 17 nm to a final value of 335 nm (data not shown) in agreement with the average of the data reported earlier [2,6,7]. This difference is a first indication suggestive of a deeper penetration in the cardiolipin system, though it should be kept in mind that depth of penetration and blue shift of fluorescence are not directly related.…”

Section: Melittin Purificationsupporting

confidence: 91%

“…Several methods to purify melittin from commercial sam-ples as well as from whole bee venom were tested. Hydrophobic interaction chromatography on Phenyl-Sepharose CL-4B and reversed phase HPLC with 5% formic acid and a gradient of isopropanol appeared to be uneffective in our hands as did gel-filtration through Sephadex G-100 [7]. Melittin without detectable phospholipase contamination could, however, be obtained both from crude melittin samples and from whole bee venom (data not shown) by reduction of the disulphide bonds of the phospholipase, followed by extraction of melittin with butanol [21].…”

Section: Melittin Purificationmentioning

confidence: 75%

“…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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“…HNP-1 has the smallest number of positively charged residues, so binding apparently results from an effective combination of hydrophobic and electrostatic forces. The binding of melittin to lipid bilayers has been studied extensively (Vogel, 1981;Bradrick & Georghiou, 1987;Beschiaschvili & Seelig, 1990). The present work suggests that the human defensins have membrane-associative properties similar to melittin.…”

Section: Forces Involved In Defensin Destabilization Of Lipid Vesiclesmentioning

confidence: 99%

Defensins promote fusion and lysis of negatively charged membranes

Fujii

Selsted

Eisenberg³

1993

Protein Science

155

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Defensins, a family of cationic peptides isolated from mammalian granulocytes and believed to permeabilize membranes, were tested for their ability to cause fusion and lysis of liposomes. Unlike a-helical peptides whose lytic effects have been extensively studied, the defensins consist primarily of 0-sheet. Defensins fuse and lyse negatively charged liposomes but display reduced activity with neutral liposomes. These and other experiments suggest that fusion and lysis is mediated primarily by electrostatic forces and to a lesser extent, by hydrophobic interactions.Circular dichroism and fluorescence spectroscopy of native defensins indicate that the amphiphilic 0-sheet structure is maintained throughout the fusion process. Taken together, these results support the idea that proteinmediated membrane fusion depends not only on hydrophobic and electrostatic forces but also on the spatial arrangement of the amino acid residues to form a three-dimensional amphiphilic structure, which promotes the efficient mixing of the lipids between membranes. A molecular model for membrane fusion by defensins is presented, which takes into account the contributions of electrostatic forces, hydrophobic interactions, and structural amphiphilicity.

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Incorporation of Melittin into phosphatidylcholine bilayers

Cited by 178 publications

References 19 publications

A molecular model for membrane fusion based on solution studies of an amphiphilic peptide from HIV gp41

A molecular model for membrane fusion based on solution studies of an amphiphilic peptide from HIV gp41

Lipid specific penetration of melittin into phospholipid model membranes

Defensins promote fusion and lysis of negatively charged membranes

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