Physicochemical studies of the protein-lipid interactions in melittin-containing micelles

Lauterwein, Jürgen; Bösch, Chris; Brown, L. R.; Wüthrich, Kurt

doi:10.1016/0005-2736(79)90046-4

Cited by 301 publications

(302 citation statements)

References 31 publications

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“…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%

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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: 51%

Section: Introductionmentioning

confidence: 99%

Incorporation of Melittin into phosphatidylcholine bilayers

Vogel¹

1981

FEBS Letters

178

119

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“…Free melittin is known to form tetramers at high concentration and high ionic strength [34]; recent fluorescence energy transfer measurements, though in principle very elegant, have led to exactly opposite conclusions [17,18] with respect to the possible multimeric state of membrane-bound melittin. From earlier 1H-NMR data [4,5], however, evidence for binding as monomers was inferred.…”

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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“…All these uncertainties prevent us from drawing quantitative conclusions about the correlation between the line widths and micellar size. Furthermore, according to Lauterwein et al (45), a variety of motions-micelle overall motion, motion of the peptide within the micelle, and motion of the hydrophobic chains within the micelle-could contribute to the observed line widths. Such complexity prevents us from deconvoluting all contributions using only the indole 1D spectrum; further data are needed to fully understand the process.…”

Section: Resultsmentioning

confidence: 90%

Structural and Dynamic Insights of the Interaction between Tritrpticin and Micelles: An NMR Study

Santos

Moraes

Nakaie

et al. 2016

Biophysical Journal

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A large number of antimicrobial peptides (AMPs) acts with high selectivity and specificity through interactions with membrane lipid components. These peptides undergo complex conformational changes in solution; upon binding to an interface, one major conformation is stabilized. Here we describe a study of the interaction between tritrpticin (TRP3), a cathelicidin AMP, and micelles of different chemical composition. The peptide's structure and dynamics were examined using one-dimensional and two-dimensional NMR. Our data showed that the interaction occurred by conformational selection and the peptide acquired similar structures in all systems studied, despite differences in detergent headgroup charge or dipole orientation. Fluorescence and paramagnetic relaxation enhancement experiments showed that the peptide is located in the interface region and is slightly more deeply inserted in 1-myristoyl-2-hydroxy-sn-glycero-3-phospho-1 0 -rac-glycerol (LMPG, anionic) than in 1-lauroyl-2-hydroxy-sn-glycero-3-phosphocholine (LLPC, zwitterionic) micelles. Moreover, the tilt angle of an assumed helical portion of the peptide is similar in both systems. In previous work we proposed that TRP3 acts by a toroidal pore mechanism. In view of the high hydrophobic core exposure, hydration, and curvature presented by micelles, the conformation of TRP3 in these systems could be related to the peptide's conformation in the toroidal pore.

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Physicochemical studies of the protein-lipid interactions in melittin-containing micelles

Cited by 301 publications

References 31 publications

Incorporation of Melittin into phosphatidylcholine bilayers

Incorporation of Melittin into phosphatidylcholine bilayers

Lipid specific penetration of melittin into phospholipid model membranes

Structural and Dynamic Insights of the Interaction between Tritrpticin and Micelles: An NMR Study

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