Effect of α-helical peptides on liposome structure: A comparative study of melittin and alamethicin

Wessman, Per; Morin, Malin; Reijmar, Karin; Edwards, Katarina

doi:10.1016/j.jcis.2010.02.032

Cited by 38 publications

(21 citation statements)

References 44 publications

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“…3A and D). According to the related literatures [9,10,17], the interaction of alamethicin with micellar carriers was closely related with the amount of peptide added into the system. It was noticed that the sizes of the complexes were affected by the ratio of alamethicin/CS-g-PSBMA: the more alamethicin was added, the smaller sizes of the complex were obtained.…”

Section: Assembly Of Alamethicin With Cs-g-psbma Micellesmentioning

confidence: 99%

“…Membrane environment significantly affects the structural properties and functionality of membrane-active peptides [3,4]. It has been realized that the reconstitution of membrane peptides in vitro is important for practical application [5][6][7][8], and many trials were performed to accommodate functions of membrane peptides with lipid bilayers [9][10][11][12][13][14][15][16][17]. However, biological lipid bilayers are often fragile and subject to disintegration when exposed to air [18,19], which limits the utilization of membrane peptides in practical devices.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Synthesis of poly(sulfobetaine methacrylate)-grafted chitosan under γ-ray irradiation for alamethicin assembly

Zhou

Dong

Wei

et al. 2015

Colloids and Surfaces B: Biointerfaces

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Section: Assembly Of Alamethicin With Cs-g-psbma Micellesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Synthesis of poly(sulfobetaine methacrylate)-grafted chitosan under γ-ray irradiation for alamethicin assembly

Zhou

Dong

Wei

et al. 2015

Colloids and Surfaces B: Biointerfaces

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“…The disks, which can be produced from lipid mixtures of various compositions and in sizes from a few tens of nanometres to several hundred nanometres [11,12], are biocompatible and show good stability against dilution. We recently presented evidence that a range of linear alpha-helical peptides, including melittin, magainin 2 and alamethicin, display high affinity for the rim of PEG-stabilized lipid disks [13]. Noteworthy, the peptides bind considerably stronger to disks than to liposomes produced from the same lipid components.…”

Section: Introductionmentioning

confidence: 99%

PEG-stabilized lipid disks as carriers for amphiphilic antimicrobial peptides

Zetterberg

Reijmar

Pränting

et al. 2011

Journal of Controlled Release

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This is an accepted version of a paper published in Journal of Controlled Release. This paper has been peer-reviewed but does not include the final publisher proof-corrections or journal pagination.Citation for the published paper: Zetterberg, M., Reijmar, K., Pränting, M., Engström, Å., Andersson, D. et al. (2011) AbstractAntimicrobial peptides hold potential as a possible alternative, or complement, to conventional antibiotics but new, safe and efficient means are needed for formulation and administration of the peptides. In this study we have investigated the utility of a novel type of lipid particles, the polyethylene glycol-stabilized lipid disks, as carriers for the model peptide melittin. The structural integrity of the carrier particle when loaded with the peptide was investigated using cryo-transmission electron microscopy. Liposome leakage upon addition of the peptide-lipid disks was monitored as a means to verify the membrane lytic effect of the formulation. The susceptibility of melittin to tryptic digestion was studied and compared in the absence and presence of lipid disks. Finally, the antibacterial effect of the peptide-lipid disk formulation was compared to that of free melittin after both single and repeated exposure to Escherichia coli. The results show that melittin can redistribute from the disk into a new host membrane and that formulation in the disks does not compromise melittin's membrane permeabilizing ability. Further, the peptide was found to be fully protected against degradation when bound to the disks. Time-kill experiments revealed that all the antibacterial effect of melittin administered in free form was gone after a single exposure to E. coli. In contrast, the disk formulation showed significant cell-killing effect also upon a second exposure to bacteria, indicating an extended release of peptide from the lipid disks. These results suggest that the lipid disks constitute a new class of promising carriers for peptide antibiotics.

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“…In contrast, the disk formulation showed significant bactericidal effect also upon a second exposure to bacteria, indicating an extended release of peptide from the lipid disks [203]. Other linear α-helical antimicrobial peptides such as magainin 2 and alamethicin also displayed high affinity for the PEG-stabilized lipid disks [204,215]. Of note, the peptides bind more strongly to disks than to liposomes produced from the same lipid components and the maximum loading capacity of the disks was superior to that of liposomes.…”

Section: Novel Formulations For Ampmentioning

confidence: 99%

“…The higher binding of the peptides to the disks compared to the liposomes is understandable from the fact that the total surface area available for the bilayer/peptide interaction is doubled using the disks instead of the closed liposomal bilayers. Further, alamethicin and magainin, similarly to melittin, have a very high affinity for curved lipid surfaces [215]. Melittin induces lipid structures with high positive curvature [216,217,218].…”

Section: Novel Formulations For Ampmentioning

confidence: 99%

Novel Formulations for Antimicrobial Peptides

Carmona-Ribeiro

Carrasco

2014

IJMS

120

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Peptides in general hold much promise as a major ingredient in novel supramolecular assemblies. They may become essential in vaccine design, antimicrobial chemotherapy, cancer immunotherapy, food preservation, organs transplants, design of novel materials for dentistry, formulations against diabetes and other important strategical applications. This review discusses how novel formulations may improve the therapeutic index of antimicrobial peptides by protecting their activity and improving their bioavailability. The diversity of novel formulations using lipids, liposomes, nanoparticles, polymers, micelles, etc., within the limits of nanotechnology may also provide novel applications going beyond antimicrobial chemotherapy.

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Effect of α-helical peptides on liposome structure: A comparative study of melittin and alamethicin

Cited by 38 publications

References 44 publications

Synthesis of poly(sulfobetaine methacrylate)-grafted chitosan under γ-ray irradiation for alamethicin assembly

Synthesis of poly(sulfobetaine methacrylate)-grafted chitosan under γ-ray irradiation for alamethicin assembly

PEG-stabilized lipid disks as carriers for amphiphilic antimicrobial peptides

Novel Formulations for Antimicrobial Peptides

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