A Biochemical And Pharmacological Characterization Of A Novel Neuroactive Peptide From The Neotropical Hunting Ant Dinoponera Australis
type: CreativeWork
description: In this investigation, venom from the giant Neotropical hunting ant Dinoponera australis (Order: Hymenoptera) has been harvested and subjected to chromatographic separations for the purpose of elucidating possible peptides that display neuroactivity by bioassay guided venom fractionation (BGVF). The venom of this arcane solitary predator paralyzes small invertebrate prey and causes highly exaggerated pain in large vertebrates. The hypothesis that the venom has a peptide component highly effective in modulating neuronal conduction by depolarization of cellular membranes has been tested and subsequent biochemical characterization has been performed to elucidate the primary structure. The data suggests that the modulation of neuronal conduction appears to result from the formation of a de novo pore that allows non-selective ion movements in a concentration dependent manner. The venom contains a variety of proteinaceous candidates and one particular peptide from the venom, -Dinoponeratoxin Da-1837, has been observed to cause very fast, large and sustained depolarization in two types of normally quiescent peripheral neurons (primary cultures of trigeminal and dorsal root ganglia) in whole cell patch clamp recordings. The profound depolarization is due to non-selective cationic flux which is irreversible at high concentrations. Preliminary studies suggest that the peptide also has a minor inhibitory effect on voltage-gated sodium channels, which does not contribute to the depolarization. Membrane assays with microsomes, fluorescent probes and lipid bilayers confirmed peptide-induced non-selective and concentration dependent permeabilization of the membrane. The primary structure of the peptide was determined by iterations of product ion scans in multiple configurations utilizing high resolution tandem mass spectrometry, commonly referred to as MS-MS data dependent acquisition. -DpTx Da-1837 is an eighteen residue peptide that is highly hydrophobic, positively charged at…
abstract: In this investigation, venom from the giant Neotropical hunting ant Dinoponera australis (Order: Hymenoptera) has been harvested and subjected to chromatographic separations for the purpose of elucidating possible peptides that display neuroactivity by bioassay guided venom fractionation (BGVF). The venom of this arcane solitary predator paralyzes small invertebrate prey and causes highly exaggerated pain in large vertebrates. The hypothesis that the venom has a peptide component highly effective in modulating neuronal conduction by depolarization of cellular membranes has been tested and subsequent biochemical characterization has been performed to elucidate the primary structure. The data suggests that the modulation of neuronal conduction appears to result from the formation of a de novo pore that allows non-selective ion movements in a concentration dependent manner. The venom contains a variety of proteinaceous candidates and one particular peptide from the venom, -Dinoponeratoxin Da-1837, has been observed to cause very fast, large and sustained depolarization in two types of normally quiescent peripheral neurons (primary cultures of trigeminal and dorsal root ganglia) in whole cell patch clamp recordings. The profound depolarization is due to non-selective cationic flux which is irreversible at high concentrations. Preliminary studies suggest that the peptide also has a minor inhibitory effect on voltage-gated sodium channels, which does not contribute to the depolarization. Membrane assays with microsomes, fluorescent probes and lipid bilayers confirmed peptide-induced non-selective and concentration dependent permeabilization of the membrane. The primary structure of the peptide was determined by iterations of product ion scans in multiple configurations utilizing high resolution tandem mass spectrometry, commonly referred to as MS-MS data dependent acquisition. -DpTx Da-1837 is an eighteen residue peptide that is highly hydrophobic, positively charged at…
author: Johnson, Stephen Roy
keywords: Mass Spectroscopy, Peptide, Toxin, Venom
date published: 2009-01-01T08:00:00Z
date modified: 2026-07-24T04:33:23Z
provider: Southern Illinois University
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: Southern Illinois University