A combined study of aggregation, membrane affinity and pore activity of natural and modified melittin

Stankowski, Stefan; Pawlak, Michael; Kaisheva, Elizabet; Robert, Charles H.; Schwarz, Gerhard

doi:10.1016/0005-2736(91)90106-i

Cited by 45 publications

(35 citation statements)

References 26 publications

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“…The melittin-induced increase in ion permeability is characterized by a fourth power dependence on melittin concentration indicating that a tetrameric structure of melittin may be responsible for channel formation (Tosteson and Tosteson, 1981;Tosteson et al 1990;Stankowski et al 1991). However, the observation that melittin exhibits multiple conductance levels in POPC (Hanke et al 1983) and asolectin (Tosteson et al 1987) membranes indicates heterogeneity in the 'pore' structure.…”

Section: Voltage-gated Channel Formationmentioning

confidence: 82%

“…Melittin disrupts the barrier function of cell membranes (Dempsey 1990;Banemann et al 1998;Epand and Vogel 1999) and has been shown to form channels in planar bilayers (Dempsey 1990;Tosteson and Tosteson 1981;Hanke et al 1983;Gevod and Birdi 1984;Tosteson et al 1985a;1987;Pawlak et al 1991;Stankowski et al 1991;Tanaka et al 1992). In the presence of a trans-negative membrane potential, melittin has been reported to induce increased permeability of ions in planar lipid membranes (Tosteson and Tosteson 1981).…”

Section: Voltage-gated Channel Formationmentioning

confidence: 95%

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Melittin: a Membrane-active Peptide with Diverse Functions

2007

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Melittin is the principal toxic component in the venom of the European honey bee Apis mellifera and is a cationic, hemolytic peptide. It is a small linear peptide composed of 26 amino acid residues in which the amino-terminal region is predominantly hydrophobic whereas the carboxy-terminal region is hydrophilic due to the presence of a stretch of positively charged amino acids. This amphiphilic property of melittin has resulted in melittin being used as a suitable model peptide for monitoring lipid-protein interactions in membranes. In this review, the solution and membrane properties of melittin are highlighted, with an emphasis on melittin-membrane interaction using biophysical approaches. The recent applications of melittin in various cellular processes are discussed.

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Section: Voltage-gated Channel Formationmentioning

confidence: 82%

Section: Voltage-gated Channel Formationmentioning

confidence: 95%

Melittin: a Membrane-active Peptide with Diverse Functions

2007

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“…This was of interest because pores formed by R-rich α-helical peptides, unlike lysine-rich peptide pores, exhibit concentration independent partition coefficients 36 and cation selectivity.…”

Section: -47mentioning

confidence: 99%

“…For example, immobilization of dianions by guanidinium cations of R-rich peptides can provide the anionic surface expected within cation selective pores. Binding of univalent anions, on the other hand, can produce the hydrophobic zwitterions compatible with negligible contributions to bilayer surface charge 36 and unhindered phase transfer.…”

Section: -47mentioning

confidence: 99%

Synthetic multifunctional pores: deletion and inversion of anion/cation selectivity using pM and pH

et al. 2003

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We report the characterization of multifunctional rigid-rod β-barrel ion channels with either internal aspartates or arginine-histidine dyads by planar bilayer conductance experiments. Barrels with internal aspartates form cation selective, large, unstable and ohmic barrel-stave (rather than toroidal) pores; addition of magnesium cations nearly deletes cation selectivity and increases single-channel stability. Barrels with internal arginine-histidine dyads form cation selective (P K ϩ/P Cl Ϫ = 2.1), small and ohmic ion channels with superb stability (single-channel lifetime > 20 seconds). Addition of "protons" results in inversion of anion/cation selectivity (P Cl Ϫ/P K ϩ = 3.8); addition of an anionic guest (HPTS) results in the blockage of anion selective but not cation selective channels. These results suggest that specific, internal counterion immobilization, here magnesium (but not sodium or potassium) cations by internal aspartates and inorganic phosphates by internal arginines (but not histidines), provides access to synthetic multifunctional pores with attractive properties.

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“…This trend was in agreement with the ICR model, i.e., the importance of intermediate internal charge repulsion for the synthesis of multifunctional pores. 24 Pore inactivation upon charge neutralization has been observed previously by Schwarz and co-workers 25 for melittin derivatives.…”

Section: Annealingmentioning

confidence: 63%

Programmed assembly of rigid-rod ?-barrel pores: Thermal inversion of chirality

Sakai

Matile

2004

Chirality

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The programmed assembly of p-octiphenyl rods carrying six complementary tripeptide strands was studied in the presence of bilayer membranes using circular dichroism (CD) spectroscopy. Thermal CD experiments demonstrated programmed assembly of anionic and cationic rods into supramolecules at low temperature that irreversibly transform into more stable supramolecules at intermediate and high temperature. Higher activation energies for programmed assembly with rods containing multiple guanidinium rather than ammonium cations was consistent with stabilization by guanidinium-anion complexes. Qualitative thermal inversion of supramolecular chirality during programmed assembly was detected continuously. Inversion of supramolecular chirality occurred with decreasing solvent polarity as well.

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A combined study of aggregation, membrane affinity and pore activity of natural and modified melittin

Cited by 45 publications

References 26 publications

Melittin: a Membrane-active Peptide with Diverse Functions

Melittin: a Membrane-active Peptide with Diverse Functions

Synthetic multifunctional pores: deletion and inversion of anion/cation selectivity using pM and pH

Programmed assembly of rigid-rod ?-barrel pores: Thermal inversion of chirality

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