Curtatoxins. Neurotoxic insecticidal polypeptides isolated from the funnel-web spider Hololena curta.

Fractionation of venom from an agelenid spider, Tegenaria agrestis, resulted in the isolation of a family of three peptides with potent insecticidal activity. These peptide toxins, TaITX‐1, ‐2, and ‐3, whose sequences were revealed from cloned cDNAs, each consist of 50 amino acid residues, six of which are cysteines. They appear to be amidated at their C‐termini and exhibit greater than 90% sequence identity. Unlike other reported spider toxins, the TaI toxins are processed from precursors containing no propeptide sequences. In lepidopteran larvae and corn rootworm beetles, the insecticidal Tegenaria toxins cause an unusual excitatory symptomatology with 50% paralytic doses ranging from 0.23 to 2.6 nmol/g. In a series of electrophysiological experiments performed in house fly larvae, these toxins caused an elevated rate of firing from central nervous system neurons. No significant effects were found when any peripheral sensory or motor systems were examined. Thus, it appears that the TaI toxins may act in a fashion not previously reported for insecticidal peptide toxins; they may act directly on the insect central nervous system. Arch. Insect Biochem. Physiol. 38:19–31, 1998. © 1998 Wiley‐Liss, Inc.

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Novel insecticidal peptides fromTegenaria agrestis spider venom may have a direct effect on the insect central nervous system

Johnson

Bloomquist

Krapcho

et al. 1998

Arch. Insect Biochem. Physiol.

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Arthropod venoms: A vast arsenal of insecticidal neuropeptides

Schwartz¹,

Mourão²,

Moreira³

et al. 2012

Biopolymers

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Arthropods are the most diverse animal group on the planet, and occupy almost all ecological niches. Venomous arthropods are a rich source of bioactive compounds evolved for prey capture and defense against predators and/or microorganisms. These highly potent chemical arsenals represent an available source for new insecticidal compounds as they act selectively on their molecular targets. These toxins affect the invertebrate nervous system and, until the moment, several insecticidal compounds belonging to the class of peptides or polyamine-like compounds have been purified and characterized from the venom of arachnids and hymenopterans. This review focuses on invertebrate-specific peptide neurotoxins that have been isolated from the venom ofspiders, scorpions, centipedes, ants, and wasps, discussing their potential in pest control and as invaluable tools in neuropharmacology.

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Solid‐Phase Synthesis and Biological Activity of a Thioether Analogue of Conotoxin G1

et al. 2003

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A bicyclic thioether analogue of alpha-conotoxin G1, a neurotoxin found in the venom of cone snails, was synthesized on solid phase. Two successive intramolecular on-bead cyclizations between a cysteine residue and a chloroacetylated reduced peptide bond are the key steps in the synthesis. The first reduced peptide bond was introduced by a reductive alkylation with a 9-fluorenylmethoxycarbonyl protected amino aldehyde, and the second by coupling of a dipeptide building block containing an allyloxycarbonyl protected reduced peptide bond. The desired bicyclic product was obtained as a mixture of two isomers, which were evaluated for their ability to inhibit the muscular nicotinic acetylcholine receptor expressed in Xenopus oocytes. The two isomers were found to have IC(50) values (inhibitory activities) of 144 microM and 48 microM, compared to 0.18 microM for native conotoxin G1.

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Curtatoxins. Neurotoxic insecticidal polypeptides isolated from the funnel-web spider Hololena curta.

Cited by 77 publications

References 24 publications

Novel insecticidal peptides fromTegenaria agrestis spider venom may have a direct effect on the insect central nervous system

Novel insecticidal peptides fromTegenaria agrestis spider venom may have a direct effect on the insect central nervous system

Arthropod venoms: A vast arsenal of insecticidal neuropeptides

Solid‐Phase Synthesis and Biological Activity of a Thioether Analogue of Conotoxin G1

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