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

Kuhn‐Nentwig, Lucia; Seebeck, Thomas; Shalaby, Tarek; Kaiser, Marcel; Nentwig, Wolfgang

doi:10.1007/s00726-009-0471-0

Cited by 40 publications

(33 citation statements)

References 49 publications

(52 reference statements)

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“…Correlation coefficients in the row charge(s)/hemolytic activity imply that positive charge of the peptides augments lytic activity and negative charge is not favorable for it (Table 5). This conclusion agrees with an observation of cupiennin-1a, revealing that reduction of sialic acids from erythrocytes also reduces the hemolytic activity of the peptide [45]. To relate the hemolytic properties of AMP with their hydrophobicity, the following approach was suggested [154].…”

Section: Hemolysissupporting

confidence: 76%

“…Some LP are bradykinin-potentiating, some possess potent insecticidal activity, and many others are cytotoxic to mammalian cells, fungi, bacteria, trypanosomes, plasmodia, or human cancer cells [6,20,28,39,[44][45][46][47][48][49]. This is probably because LP are rather flexible and can interact with a plethora of biological molecules, ranging from lipids and carbohydrates to proteins and nucleic acids (Fig.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Hemolysissupporting

confidence: 76%

Section: Introductionmentioning

confidence: 99%

Latarcins: versatile spider venom peptides

Dubovskii

Vassilevski

Kozlov

et al. 2015

Cell. Mol. Life Sci.

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“…In addition to antimicrobial activities, this peptide also displayed insecticidal activity, which might be helpful for capturing the prey. Like hadrurin [37], synthesis of cupiennin 1a in all L- or D-amino acids led to similar activity, implying membrane targeting rather than the use of chiral targets such as receptors [62]. NMR studies [54] revealed a helix-hinge-helix structure (Figure 1C).…”

Section: Spider Antimicrobial Peptidesmentioning

confidence: 99%

“…NMR studies [54] revealed a helix-hinge-helix structure (Figure 1C). Such a structure is responsible for antimicrobial activity of the peptide against E. coli, Pseudomonas aeruginosa, S. aureus , and Enterococcus faecalis at very low concentrations (0.31–5.00 µM) [14, 62]. In particular, it has a more hydrophobic N-terminus characterized by three aromatic phenylalanines (Table 3).…”

Section: Spider Antimicrobial Peptidesmentioning

confidence: 99%

Insights into Antimicrobial Peptides from Spiders and Scorpions

Wang¹,

Wang

2016

PPL

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The venoms of spiders and scorpions contain a variety of chemical compounds. Antimicrobial peptides (AMPs) from these organisms were first discovered in the 1990s. As of May 2015, there were 42 spider’s and 63 scorpion’s AMPs in the Antimicrobial Peptide Database (http://aps.unmc.edu/AP). These peptides have demonstrated broad or narrow-spectrum activities against bacteria, fungi, viruses, and parasites. In addition, they can be toxic to cancer cells, insects and erythrocytes. To provide insight into such an activity spectrum, this article discusses the discovery, classification, structure and activity relationships, bioinformatics analysis, and potential applications of spider and scorpion AMPs. Our analysis reveals that, in the case of linear peptides, spiders use both glycine-rich and helical peptide models for defense, whereas scorpions use two distinct helical peptide models with different amino acid compositions to exert the observed antimicrobial activities and hemolytic toxicity. Our structural bioinformatics study improves the knowledge in the field and can be used to design more selective peptides to combat tumors, parasites, and viruses.

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“…Antimicrobial Activity-Antimicrobial activity of CsTx-1, CsTx-2a, CT1-long, and CT1-short against Escherichia coli ATCC 25922, E. coli souchier bactériologique de Saclay (SBS) 363, Staphylococcus aureus ATCC 29213, and Trypanosoma brucei brucei MiTat1.2(221) were determined as described in Kuhn-Nentwig et al (21).…”

Section: Methodsmentioning

confidence: 99%

A Venom-derived Neurotoxin, CsTx-1, from the Spider Cupiennius salei Exhibits Cytolytic Activities

Kuhn‐Nentwig

Федорова

Lüscher

et al. 2012

Journal of Biological Chemistry

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Background: CsTx-1, an ICK motif containing neurotoxin, acts as L-type Ca 2ϩ -channel inhibitor. Results: The partial ␣-helical C terminus of CsTx-1 exhibits cytolytic activity toward prokaryotic and eukaryotic cell membranes. Conclusion: CsTx-1 is one peptide with different domains for ion channel inhibition and cytolytic activity. Significance: Shown is an important new mechanism for the evolution of spider venomous peptides.

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

Cited by 40 publications

References 49 publications

Latarcins: versatile spider venom peptides

Latarcins: versatile spider venom peptides

Insights into Antimicrobial Peptides from Spiders and Scorpions

A Venom-derived Neurotoxin, CsTx-1, from the Spider Cupiennius salei Exhibits Cytolytic Activities

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