Conformation and lytic activity of eumenine mastoparan: a new antimicrobial peptide from wasp venom

Cabrera, Marcia Perez dos Santos; Souza, Bibiana Monson de; Fontana, Renato; Konno, Katsuhiro; Palma, Mário Sérgio; Azevedo, Walter Filgueira de; Neto, João Ruggiero

doi:10.1111/j.1399-3011.2004.00173.x

Cited by 56 publications

(42 citation statements)

References 38 publications

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“…It has been established that at a given MLT concentration after the formation process the pores are stable (Ladokhin et al 1997;Yang et al 2001;Naito et al 2000;Chen et al 2003;dos Santos Cabrera et al 2004;Huang et al 2004;Allende et al 2005;Macháň et al 2010); however, in our previous work with single giant vesicles, we investigated the interactions between the vesicles and MLT, and showed that in a wide range of MLT concentrations the MLT-induced membrane permeability is increasing with MLT concentration and also with time at a given concentration (Mally et al 2007). Namely, the osmotically tensed vesicles underwent a series of bursts, with vesicle membrane resealing after each burst.…”

Section: Introductionmentioning

confidence: 95%

The dynamics of melittin-induced membrane permeability

2012

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The transport of co-encapsulated solutes through the melittin-induced pores in the membrane of giant phospholipid vesicles was studied, and the characteristics of the pore formation process were modeled. Molecules of two different sizes (dextran and the smaller, fluorescent marker Alexa Fluor) were encapsulated inside the vesicles. The chosen individual vesicles were then transferred by micromanipulation from the stock suspension to the environment with the melittin (MLT). The vesicles were observed optically with a phase-contrast microscope and by monitoring the fluorescence signal. Such an experimental setup enabled an analysis of a single vesicle's response to the MLT on the basis of simultaneous, separate measurements of the outflow of both types of encapsulated molecules through the MLT-induced pores in the membrane. The mechanisms of the MLT's action were suggested in a model for MLT pore formation, with oligomeric pores continuously assembling and dissociating in the membrane. Based on the model, the results of the experiments were explained as a consequence of the membrane's permeability dynamics, with a continuously changing distribution of pores in the membrane with regard to their size and number. The relatively stable "average MLT pore" characteristics can be deduced from the proposed model.

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Section: Introductionmentioning

confidence: 95%

The dynamics of melittin-induced membrane permeability

2012

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“…The hydrophobic nature of most of the amino acid residues in mastoparans usually leads them to adopt amphipathic α-helical conformations in micellar solvents [5] and in a membrane-bound state [6]. The cationicity of mastoparans contributes to the formation of discriminate anionic vesicles, which favor their antimicrobial activity [7][8][9].…”

Section: Introductionmentioning

confidence: 99%

“…It was previously reported that the deamidation of the C-terminus of the membrane-active peptide EMP-AF1 reduces its antimicrobial potency [5], while suppressing its hemolytic activity [14].…”

Section: Introductionmentioning

confidence: 99%

The effects of the C-terminal amidation of mastoparans on their biological actions and interactions with membrane-mimetic systems

Silva

Souza

Cabrera

et al. 2014

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Polycationic peptides may present their C-termini in either amidated or acidic form; however, the effects of these conformations on the mechanisms of interaction with the membranes in general were not properly investigated up to now. Protonectarina-MP mastoparan with an either amidated or acidic C-terminus was utilized to study their interactions with anionic and zwitterionic vesicles, using measurements of dye leakage and a combination of H/D exchange and mass spectrometry to monitor peptide-membrane interactions. Mast cell degranulation, hemolysis and antibiosis assays were also performed using these peptides, and the results were correlated with the structural properties of the peptides. The C-terminal amidation promotes the stabilization of the secondary structure of the peptide, with a relatively high content of helical conformations, permitting a deeper interaction with the phospholipid constituents of animal and bacterial cell membranes. The results suggested that at low concentrations Protonectarina-MP interacts with the membranes in a way that both terminal regions remain positioned outside the external surface of the membrane, while the α-carbon backbone becomes partially embedded in the membrane core and changing constantly the conformation, and causing membrane destabilization. The amidation of the C-terminal residue appears to be responsible for the stabilization of the peptide conformation in a secondary structure that is richer in α-helix content than its acidic congener. The helical, amphipathic conformation, in turn, allows a deeper peptide-membrane interaction, favoring both biological activities that depend on peptide structure recognition by the GPCRs (such as exocytosis) and those activities dependent on membrane perturbation (such as hemolysis and antibiosis).

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“…Mastoparan has been shown to take the ␣-helical conformation upon binding with phospholipid membrane (37) and to cause liposome permeabilization in a transmembrane potential-dependent manner (36) that seems to be the mechanism for mitochondria as well (38). Recently, it has been shown that the liposome permeation ability of eumenine mastoparan, a novel natural tetradecapeptide with a broad-spectrum inhibitory activity against Gram-positive and Gram-negative bacteria, is correlated with the amount of helical conformation in the membrane (39).…”

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confidence: 99%

Mitochondria Permeabilization by a Novel Polycation Peptide BTM-P1

Lemeshko

Arias

Ordúz

2005

Journal of Biological Chemistry

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Bacillus thuringiensis subsp. medellin is known to produce the Cry11Bb protein of 94 kDa, which is toxic for mosquito larvae due to permeabilization of the plasma membrane of midgut epithelial cells. Earlier we found that a 2.8-kDa novel peptide BTM-P1, which was artificially synthesized taking into account the primary structure of Cry11Bb endotoxin, is active against several species of bacteria. In this work we show that BTM-P1 induces cyclosporin A-insensitive swelling of rat liver mitochondria in various salt solutions but not in the sucrose medium. Inorganic phosphate and Ca 2؉ significantly increased this effect of the peptide. The uncoupling action of BTM-P1 on oxidative phosphorylation was stronger in the potassiumcontaining media and correlated with a decrease of the inner membrane potential of mitochondria. In isotonic KNO 3 , KCl, or NH 4 NO 3 media, a complete drop of the inner membrane potential was observed at 1-2 g/ml of the peptide. The peptide-induced swelling was increased by energization of mitochondria in the potassium-containing media, but it was inhibited in the NaNO 3 , NH 4 NO 3 , and Tris-NO 3 media. All mitochondrial effects of the peptide were completely prevented by adding a single N-terminal tryptophan residue to the peptide sequence. We suggest a mechanism of membrane permeabilization that includes a transmembrane-and surface potential-dependent insertion of the polycation peptide into the lipid bilayer and its oligomerization leading to formation of ion channels and also to the mitochondrial permeability transition pore opening in a cyclosporin A-insensitive manner.

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Conformation and lytic activity of eumenine mastoparan: a new antimicrobial peptide from wasp venom

Cited by 56 publications

References 38 publications

The dynamics of melittin-induced membrane permeability

The dynamics of melittin-induced membrane permeability

The effects of the C-terminal amidation of mastoparans on their biological actions and interactions with membrane-mimetic systems

Mitochondria Permeabilization by a Novel Polycation Peptide BTM-P1

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