The orientation of melittin in lipid membranes. A polarized infrared spectroscopy study

Vogel, Horst; Jähnig, Fritz; Hoffmann, Volker; Stümpel, J.

doi:10.1016/0005-2736(83)90523-0

Cited by 88 publications

(48 citation statements)

References 29 publications

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“…A number of lipid-associating amphipathic peptides are known to self-associate on the lipid surface, including the closely related 18A peptide (8), the bee venom toxin melittin (36,37), and the antibiotic alamethicin (39). However, the half-life of the active ester of DSS in aqueous solution is approximately 4 -5 h at pH 7.0 and 0°C (39).…”

Section: Discussionmentioning

confidence: 99%

Mass Spectrometry to Characterize the Binding of a Peptide to a Lipid Surface

MacPhee

Howlett

Sawyer

1999

Analytical Biochemistry

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Section: Discussionmentioning

confidence: 99%

Mass Spectrometry to Characterize the Binding of a Peptide to a Lipid Surface

MacPhee

Howlett

Sawyer

1999

Analytical Biochemistry

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“…On basis of the expected amphipathicity [3,8] of the helices that are formed during binding to phospholipids [7,35] some authors [8,3] have proposed that the orientation of the melittin molecule is parallel to the membrane surface, perhaps with the exception of the smaller C-terminal helix 15-21 [3]. Polarized infrared spectroscopy studies [15], however, have provided experimental evidence in favour of a mean orientation of the helices perpendicular to the plane of the bilayer, as a result of either a transmembrane orientation as suggested earlier [9] or a 'loop'-orientation with Cand N-terminus at the same side of the lipid layer involving a sharp nick around residue 13, a model supported also by others [10] on basis of proton NMR studies.…”

Section: Discussionmentioning

confidence: 99%

“…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%

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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“…Alternatively, lytic peptides can bind via hydrophobic interactions with membranes to form transmembrane channels/pores via the 'barrel-stave' mechanism ( fig. 1) [59,60]. However, in contrast to peptides that act via the carpet mechanism, such peptides have been shown to be non-cell-selective and also lyse normal cells [43,61,62].…”

Section: Different Mechanisms For Cell Killingmentioning

confidence: 97%

Host defense peptides as new weapons in cancer treatment

Papo

Shai

2005

CMLS, Cell. Mol. Life Sci.

439

388

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In the last decade intensive research has been conducted to determine the role of innate immunity host defense peptides (also termed antimicrobial peptides) in the killing of prokaryotic and eukaryotic cells. Many antimicrobial peptides damage the cellular membrane as part of their killing mechanism. However, it is not clear what makes cancer cells more susceptible to some of these peptides, and what the molecular mechanisms underlying these activities are. Two general mechanisms were suggested: (i) plasma membrane disruption via micellization or pore formation, and (ii) induction of apoptosis via mitochondrial membrane disruption. To be clinically used, these peptides need to combine high and specific anticancer activity with stability in serum. Although so far very limited, new studies have paved the way for promising anticancer host defense peptides with a new mode of action and with a broad spectrum of anticancer activity.

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The orientation of melittin in lipid membranes. A polarized infrared spectroscopy study

Cited by 88 publications

References 29 publications

Mass Spectrometry to Characterize the Binding of a Peptide to a Lipid Surface

Mass Spectrometry to Characterize the Binding of a Peptide to a Lipid Surface

Lipid specific penetration of melittin into phospholipid model membranes

Host defense peptides as new weapons in cancer treatment

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