Publications by authors named "S Peigneur"
Article Synopsis
- The stonefish species Synanceia verrucosa and Synanceia horrida are among the most venomous fish, known for causing severe stings in humans, prompting research into their venom components.
- This study shifted focus from proteins to small molecules in stonefish venom and identified three new substances: γ-aminobutyric acid (GABA), choline, and 0-acetylcholine, with GABA being the first of its kind found in fish venom.
- The research revealed how these venoms activate specific human receptors and demonstrated distinct cytotoxic effects, suggesting a need for further exploration of these small molecules to improve understanding and treatment of sting-related symptoms.
Background: The identification of novel toxins from overlooked and taxonomically exceptional species bears potential for various pharmacological applications. The remipede Xibalbanus tulumensis, an underwater cave-dwelling crustacean, is the only crustacean for which a venom system has been described. Its venom contains several xibalbin peptides that have an inhibitor cysteine knot (ICK) scaffold.
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- Lepidopterism, caused by exposure to hairs from processionary caterpillars, is emerging as a public health issue due to increasing outbreaks, particularly linked to climate change.
- Current treatments only aim to relieve symptoms since there is no effective cure, and the precise mechanisms of how symptoms arise are not fully understood.
- A recent study identified 171 venom components from the oak processionary caterpillar, providing crucial insights for developing better therapeutic strategies against lepidopterism.
As human skin comes into contact with the tiny hairs or setae of the oak processionary caterpillar, Thaumetopoea processionea, a silent yet intense chemical confrontation occurs. The result is a mix of issues: skin rashes and an intense itching that typically lasts days and weeks after the contact. This discomfort poses a significant health threat not only to humans but also to animals.
View Article and Find Full Text PDFAn insect neuroactive helix ring peptide called U-MYRTX-Tb1a (abbreviated as U) from the venom of the ant, . U is a 34-amino-acid peptide that is claimed to be one of the most paralytic peptides ever reported from ant venoms acting against blowflies and honeybees. The peptide features a compact triangular ring helix structure stabilized by a single disulfide bond, which is a unique three-dimensional scaffold among animal venoms.
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