Synthesis of Reversed Magainin 2 Analogs Enhanced Antibacterial Activity.

Iwahori, Akiyo; Hirota, Yukiko; Sampe, Ruriko; Miyano, Sanae; Numao, Naganori

doi:10.1248/bpb.20.267

Cited by 17 publications

(18 citation statements)

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“…This result is consistent with that of the antimicrobial activity of magainin 2 and its analogs in human red blood and bacteria cells. 21 Using the pore diameter and the monomer size from the Protein Data Bank (PDB), the number of assembling monomers was mathematically calculated by…”

Section: Resultsmentioning

confidence: 99%

Channel Current Analysis for Pore-forming Properties of an Antimicrobial Peptide, Magainin 1, Using the Droplet Contact Method

Watanabe

Kawano

2016

ANAL. SCI.

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This study describes the pore-forming properties of magainin 1 in planar lipid bilayers. These bilayers were prepared by the droplet contact method, which was executed on a microfabricated device for a high-throughput study. We arrayed four droplet chambers parallelly in the single device, and the current measurements were carried out simultaneously. Using this system, we measured the channel current conductance of magainin 1. We determined the pore size and the number of assembling monomers in magainin pores in mammalian and bacterial model membranes. This system is a powerful tool for analyzing transmembrane peptides and their antimicrobial activities.

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Section: Resultsmentioning

confidence: 99%

Channel Current Analysis for Pore-forming Properties of an Antimicrobial Peptide, Magainin 1, Using the Droplet Contact Method

Watanabe

Kawano

2016

ANAL. SCI.

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“…15,48,118 It has also been shown that retro analogues of MSI 78 maintain antibacterial activity with reduced hemolytic activity. 156 This indicates that it is the overall amphipathic structure, rather than specific stereochemistry or amide bond direction, that determines activity, as long as these modifications do not affect structuring. 119 The introduction of single or double D-amino acid substitutions, which lead to destructuring, instead markedly modulate both antibacterial and hemolytic activities.…”

Section: Sequence Modification Methodsmentioning

confidence: 99%

Amphipathic, α-helical antimicrobial peptides

2000

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“…There are many examples that the reversed analogs of antimicrobial peptides posses equal or enhanced antimicrobial activities (16). While viewing the amino acid sequence and the solution structure of Pac-525, it was noticed that the reversed sequence of Pac-525, Ac-IWRVWRRWK-NH 2 , designated Pac-525 rev , may also possess the antimicrobial activity.…”

Section: Vol 188 2006mentioning

confidence: 99%

Solution Structure of a Novel Tryptophan-Rich Peptide with Bidirectional Antimicrobial Activity

Wei

Kuo

et al. 2006

J Bacteriol

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Trp-rich antimicrobial peptides play important roles in the host innate defense mechanisms of many plants, insects, and mammals. A new type of Trp-rich peptide, Ac-KWRRWVRWI-NH 2 , designated Pac-525, was found to possess improved activity against both gram-positive and -negative bacteria. We have determined that the solution structures of Pac-525 bound to membrane-mimetic sodium dodecyl sulfate (SDS) micelles. The SDS micelle-bound structure of Pac-525 adopts an ␣-helical segment at residues Trp2, Arg3, and Arg4. The positively charged residues are clustered together to form a hydrophilic patch. The three hydrophobic residues Trp2, Val6, and Ile9 form a hydrophobic core. The surface electrostatic potential map indicates the three tryptophan indole rings are packed against the peptide backbone and form an amphipathic structure. Moreover, the reverse sequence of Pac-525, Ac-IWRVWRRWK-NH 2 , designated Pac-525 rev , also demonstrates similar antimicrobial activity and structure in membrane-mimetic micelles and vesicles. A variety of biophysical and biochemical methods, including circular dichroism, fluorescence spectroscopy, and microcalorimetry, were used to show that Pac-525 interacted strongly with negatively charged phospholipid vesicles and induced efficient dye release from these vesicles, suggesting that the antimicrobial activity of Pac-525 may be due to interactions with bacterial membranes.

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Synthesis of Reversed Magainin 2 Analogs Enhanced Antibacterial Activity.

Cited by 17 publications

References 0 publications

Channel Current Analysis for Pore-forming Properties of an Antimicrobial Peptide, Magainin 1, Using the Droplet Contact Method

Channel Current Analysis for Pore-forming Properties of an Antimicrobial Peptide, Magainin 1, Using the Droplet Contact Method

Amphipathic, α-helical antimicrobial peptides

Solution Structure of a Novel Tryptophan-Rich Peptide with Bidirectional Antimicrobial Activity

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