The interaction of bee melittin with lipid bilayer membranes

Dawson, Charles R.; Drake, Alex F.; Helliwell, Jack; Hider, Robert C.

doi:10.1016/0005-2736(78)90131-1

Cited by 258 publications

(138 citation statements)

References 39 publications

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“…Quantitatively, a melittin molecule, bound to lipid membranes, shows a conformation with ~70% c~-belical content corresponding to 18-19 amino acids. According to a Chou-Fasman analysis, the hydrophobic segment of melittin is predicted to be c~-helical andfc ~ = 0.65 [6,12] agreement with our experimental data with DMPC. Because of the Pro14 residue, however, which generally is known to be a helix breaker [12], at least two helical segments exist in a membrane associated melittin molecule.…”

Section: Binding Of Melittin To Dmpc Membranes Determined By CD Measusupporting

confidence: 83%

“…We have observed comparable results with negatively charged lipid membranes of dimyristoylmethylphosphatidic acid (fa = 0.72) and micelles of the detergent SDS (f~ = 0.74), indicating that the conformation is rather independent of the lipid headgroup. Our result on SDS agrees with the CD data of detergent-melittin complexes of other groups [6,7], but is in conflict with a value offa = 1.07 reported in [8].…”

Section: Binding Of Melittin To Dmpc Membranes Determined By CD Measusupporting

confidence: 51%

“…It is known that in an aqueous solution of low concentration and low ionic strength melittin adopts a mainly random conformation. Upon interaction with various detergent molecules or lipid membranes a conformational change to a mainly a-helical structure has been observed [4][5][6][7][8]. The binding of melittin to lipid membranes is accompanied by a change of the spectral properties of the single fluorescent residue Trpl 9 [2--5,9,10].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Incorporation of Melittin into phosphatidylcholine bilayers

Vogel¹

1981

FEBS Letters

178

119

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Section: Binding Of Melittin To Dmpc Membranes Determined By CD Measusupporting

confidence: 83%

Section: Binding Of Melittin To Dmpc Membranes Determined By CD Measusupporting

confidence: 51%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Incorporation of Melittin into phosphatidylcholine bilayers

Vogel¹

1981

FEBS Letters

178

119

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“…This model is reminiscent of the wedge models proposed for a-helical peptides, such as melittin (Dawson et al, 1978;Terwilliger et al, 1982;Batenburg & de Kruiff, 1988) or SI (Fujii et al, 1992). If the defensin dimer is imagined to be an amphiphilic wedge, then Figure 7C illustrates the similarity of the defensins to the wedges formed by an a-helix.…”

Section: A Speculative Model For Defensin-induced Membrane Fusionmentioning

confidence: 93%

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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“…8A). The a-helical region of the peptide then embeds itself in the membrane surface, probably in a wedge type of interaction (Dawson et al, 1978;Terwilliger et al, 1982;Batenburg & de Kruiff, 1988). Fusion between liposomes occurs because some of the positively charged residues interact with other liposomes thus bringing them into close contact with one another (Fig.…”

Section: A Speculative Molecular Model For Peptide-induced Fusionmentioning

confidence: 99%

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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The interaction of bee melittin with lipid bilayer membranes

Cited by 258 publications

References 39 publications

Incorporation of Melittin into phosphatidylcholine bilayers

Incorporation of Melittin into phosphatidylcholine bilayers

Defensins promote fusion and lysis of negatively charged membranes

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

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