Membranolytic antifungal activity of arenicin-1 requires the N-terminal tryptophan and the beta-turn arginine

Park, Cana; Cho, Jae-Yong; Lee, Jun-Young; Lee, Dong Gun

doi:10.1007/s10529-010-0402-x

Cited by 14 publications

(8 citation statements)

References 15 publications

(18 reference statements)

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“…Similarly, when the Gly10 was replaced with Asp, the β-turn structure of peptide L1 was destroyed, which also caused a sharp decrease in the antimicrobial activity of L1 (Table 3), therefore suggesting that the β-turn of L1 could also be the functional domain of this antibacterial peptide. A similar observation was also previously reported by Park et al (2011). Thus, based on the mutational analysis of L1, it could be classified as an α-helical β-turn antimicrobial peptide (Yang et al 2002).…”

Section: Discussionsupporting

confidence: 92%

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei

et al. 2018

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Hemocyanin, the multifunctional glycoprotein in the hemolymph of invertebrates, can generate various antimicrobial peptides (AMPs). Given the rising interest in the use of natural therapeutic agents such as AMPs, alternative and more efficient methods for their generation are being explored. In this work, free online software was first applied to predict the generation of antimicrobial peptides from the large subunit of Litopenaeus vannamei hemocyanin. Twenty potential antimicrobial peptides ranging from 1.5 to 1.9 kDa were predicted, five of which had α-helical structures and were selected for antibacterial activity testing. The results indicated that these five peptides had antibacterial activity against seven different bacteria. Of the five peptides, one peptide, designated L1, had the strongest antibacterial activity against both Gram-negative and Gram-positive bacteria. Moreover, CD and NMR data showed that L1 had both α-helical and β-turns structural composition, and that these structures were essential for L1’s antibacterial activity. Furthermore, SEM analysis revealed that peptide L1 had broad-spectrum activity against both Gram-positive and Gram-negative bacteria, as it could destroy the bacterial cell walls and kill the bacteria. Thus, L1 is a very potent antimicrobial peptide that can be exploited and used in antibacterial therapeutics.Electronic supplementary materialThe online version of this article (10.1007/s00726-018-2575-x) contains supplementary material, which is available to authorized users.

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Section: Discussionsupporting

confidence: 92%

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei

et al. 2018

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“…However, it also displays a substantial cytotoxicity towards mammalian cells [1,2,3]. The mechanism of antimicrobial action of arenicin-1 is associated with a distinctive membranolytic activity [5,6,7,8,9,10,11,12]. Its potent antibiotic activity makes this peptide a fascinating lead for designing variants to test which features determine the antimicrobial and/or cytotoxic capacities and to disclose if they can be in some way extricated.…”

Section: Introductionmentioning

confidence: 99%

Redesigning Arenicin-1, an Antimicrobial Peptide from the Marine Polychaeta Arenicola marina, by Strand Rearrangement or Branching, Substitution of Specific Residues, and Backbone Linearization or Cyclization

et al. 2019

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Arenicin-1, a β-sheet antimicrobial peptide isolated from the marine polychaeta Arenicola marina coelomocytes, has a potent, broad-spectrum microbicidal activity and also shows significant toxicity towards mammalian cells. Several variants were rationally designed to elucidate the role of structural features such as cyclization, a certain symmetry of the residue arrangement, or the presence of specific residues in the sequence, in its membranolytic activity and the consequent effect on microbicidal efficacy and toxicity. The effect of variations on the structure was probed using molecular dynamics simulations, which indicated a significant stability of the β-hairpin scaffold and showed that modifying residue symmetry and β-strand arrangement affected both the twist and the kink present in the native structure. In vitro assays against a panel of Gram-negative and Gram-positive bacteria, including drug-resistant clinical isolates, showed that inversion of the residue arrangement improved the activity against Gram-negative strains but decreased it towards Gram-positive ones. Variants with increased symmetry were somewhat less active, whereas both backbone-cyclized and linear versions of the peptides, as well as variants with R→K and W→F replacement, showed antimicrobial activity comparable with that of the native peptide. All these variants permeabilized both the outer and the inner membranes of Escherichia coli, suggesting that a membranolytic mechanism of action was maintained. Our results indicate that the arenicin scaffold can support a considerable degree of variation while maintaining useful biological properties and can thus serve as a template for the elaboration of novel anti-infective agents.

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“…Length and degree of saturation of the lipid hydrocarbon tails play a significant role in membrane viscoelastic properties for both mammalian and bacterial cells. In natural membranes, usually an even number of C atoms exists in the hydrocarbon chains, hence lauroyl (12:0), myristoyl (14:0), palmitoyl (16:0), stearoyl (18:0), arachidoyl (20:0), oleoyl (18:1c), linoleoyl (18:2 cm 3 , ), arachidonoyl (20:4cccc ,,, ), and so forth are used in model systems. For some methods (e.g., GIXD) the most convenient objects are the fully saturated phospholipids, which can easily form a condensed (liquid-crystalline) state at room temperature and are characterized by well-defined phase transitions.…”

Section: Introductionmentioning

confidence: 99%

“…The present study is focused on the recently discovered peptide arenicin-1 (Ar-1), which possesses antibacterial and antifungal activities. − Two isoforms with only one difference in an amino acid residue have been originally isolated from lugworm Arenicola marina . Ar-1 consists of 21 amino acid residues, 6 of which are positively charged arginines and 2 sulfur-containing cysteines causing the large 18-residue portion to loop, folding into a unique twisted beta-sheet structure, exposing an amphipathic surface .…”

Section: Introductionmentioning

confidence: 99%

Influence of Arenicin on Phase Transitions and Ordering of Lipids in 2D Model Membranes

et al. 2013

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Antimicrobial peptides (AMPs) are important effector molecules of the innate immune system of all species. AMPs are highly selective and can be used as lead structures for the development of new drugs complementing standard antibiotic therapies. Understanding the crucial parameters of peptide-membrane interactions is necessary for elucidation of the molecular mechanisms of action. Phospholipid monolayers, as simple 2D models of the membrane surface, can be effectively used for studies of peptide-membrane interactions. The present study is focused on the recently discovered peptide arenicin-1 (Ar-1), which possesses antibacterial and antifungal activities. A linear derivative with serine residues instead of cysteines (C/S-Ar-1) was additionally used to investigate the influence of the AMP on the phase behavior of lipid monolayers at the air/liquid interface. Using the Langmuir balance technique and IRRAS allows us to conclude that both original and modified arenicins reveal a strong influence on the phase transition of anionic phospholipids (fluidization of the lipid hydrocarbon chains), whereas the thermodynamic properties of the zwitterionic phospholipid layers are not affected. A strong effect of the modified peptide on the ordering of negatively charged phospholipids at the air-water interface compared to zwitterionic phospholipids has been observed using GIXD measurements, supported by IRRAS simulations for the spectral range corresponding to the lipid hydrocarbon chains. At lateral pressures above 30 mN/m, both peptides are squeezed out from zwitterionic lipid monolayers, but remains attached to and partly incorporated in anionic lipid monolayers. This study points at the importance of the interplay between hydrophobic and electrostatic interactions for the membrane disruption by AMPs.

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Membranolytic antifungal activity of arenicin-1 requires the N-terminal tryptophan and the beta-turn arginine

Cited by 14 publications

References 15 publications

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei

Redesigning Arenicin-1, an Antimicrobial Peptide from the Marine Polychaeta Arenicola marina, by Strand Rearrangement or Branching, Substitution of Specific Residues, and Backbone Linearization or Cyclization

Influence of Arenicin on Phase Transitions and Ordering of Lipids in 2D Model Membranes

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