Cupiennin 1a, an antimicrobial peptide from the venom of the neotropical wandering spider <i>Cupiennius salei</i>, also inhibits the formation of nitric oxide by neuronal nitric oxide synthase

Pukala, Tara L.; Doyle, Jason; Llewellyn, Lyndon; Kuhn‐Nentwig, Lucia; Apponyi, Margit A.; Separovic, Frances; Bowie, John H.

doi:10.1111/j.1742-4658.2007.05726.x

Cited by 25 publications

(12 citation statements)

References 36 publications

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“…Remarkably, Cu1a exhibits a second, non-membranolytic activity: in the submicromolar range, the peptide inhibits the formation of nitric oxide by neuronal nitric oxide synthase through complexation with the regulatory protein Ca 2? calmodulin (Pukala et al 2007b). This indicates that the targets of Cu1a in a spider's prey are not only the cell membranes, but also cellular enzymes.…”

Section: Introductionmentioning

confidence: 98%

Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells

et al. 2010

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Cupiennin 1a, a cytolytic peptide isolated from the venom of the spider Cupiennius salei, exhibits broad membranolytic activity towards bacteria, trypanosomes, and plasmodia, as well as human blood and cancer cells. In analysing the cytolytic activity of synthesised all-D-and all-L-cupiennin 1a towards pro-and eukaryotic cells, a stereospecific mode of membrane destruction could be excluded. The importance of negatively charged sialic acids on the outer leaflet of erythrocytes for the binding and haemolytic activity of L-cupiennin 1a was demonstrated. Reducing the overall negative charges of erythrocytes by partially removing their sialic acids or by protecting them with tri-or pentalysine results in reduced haemolytic activity of the peptide.

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Section: Introductionmentioning

confidence: 98%

Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells

et al. 2010

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“…Antimicrobial peptides serve as a first line of defense against invading pathogens, and are involved in modulating the host signaling mechanisms of the immune response [2]. Previous studies have shown that several antimicrobial peptides inhibit the formation of nitric oxide by interacting with or affecting nitric oxide synthase; such peptides include caerin [3e5], cupiennin [6], dahlein [5], frenatin [5,7], and citropin [8]. An a-helical antimicrobial peptide, named moronecidin or piscidin (PCD)-1, was previously isolated from the skin and gills of hybrid striped bass [1].…”

Section: Introductionmentioning

confidence: 99%

The use of the antimicrobial peptide piscidin (PCD)-1 as a novel anti-nociceptive agent

Chen¹,

Huang²,

Liao³

et al. 2015

Biomaterials

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“…Of note, membranolytic activity was reported for cytolytic LP. In addition, cupiennin 1a was shown to inhibit nitric oxide formation by neuronal nitric oxide synthase through complexation with the regulatory protein calmodulin [50].…”

Section: Introductionmentioning

confidence: 99%

Latarcins: versatile spider venom peptides

Dubovskii

Vassilevski

Kozlov

et al. 2015

Cell. Mol. Life Sci.

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Arthropod venoms feature the presence of cytolytic peptides believed to act synergetically with neurotoxins to paralyze prey or deter aggressors. Many of them are linear, i.e., lack disulfide bonds. When isolated from the venom, or obtained by other means, these peptides exhibit common properties. They are cationic; being mostly disordered in aqueous solution, assume amphiphilic α-helical structure in contact with lipid membranes; and exhibit general cytotoxicity, including antifungal, antimicrobial, hemolytic, and anticancer activities. To suit the pharmacological needs, the activity spectrum of these peptides should be modified by rational engineering. As an example, we provide a detailed review on latarcins (Ltc), linear cytolytic peptides from Lachesana tarabaevi spider venom. Diverse experimental and computational techniques were used to investigate the spatial structure of Ltc in membrane-mimicking environments and their effects on model lipid bilayers. The antibacterial activity of Ltc was studied against a panel of Gram-negative and Gram-positive bacteria. In addition, the action of Ltc on erythrocytes and cancer cells was investigated in detail with confocal laser scanning microscopy. In the present review, we give a critical account of the progress in the research of Ltc. We explore the relationship between Ltc structure and their biological activity and derive molecular characteristics, which can be used for optimization of other linear peptides. Current applications of Ltc and prospective use of similar membrane-active peptides are outlined.

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Cupiennin 1a, an antimicrobial peptide from the venom of the neotropical wandering spider Cupiennius salei, also inhibits the formation of nitric oxide by neuronal nitric oxide synthase

Cited by 25 publications

References 36 publications

Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells

Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells

The use of the antimicrobial peptide piscidin (PCD)-1 as a novel anti-nociceptive agent

Latarcins: versatile spider venom peptides

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