The new peptide from the Fea’s viper Azemiops feae venom interacts with nicotinic acetylcholine receptors

Utkin, Yuri N.; Weise, Christoph; Anh, Hoang Ngoc; Kasheverov, Igor E.; Starkov, Vladislav G.; Tsetlin, Victor I.

doi:10.1134/s1607672912010103

Cited by 4 publications

(1 citation statement)

References 9 publications

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“…Earlier, we purified the 2540-Da polypeptide azemiopsin from A. feae venom (15). In this paper we describe the determination of its amino acid sequence and biological activity of azemiopsin; like waglerins, azemiopsin selectively blocks muscle-type nAChR but has a markedly different primary structure and does not contain disulfide bridges.…”

Section: Introductionmentioning

confidence: 99%

Azemiopsin from Azemiops feae Viper Venom, a Novel Polypeptide Ligand of Nicotinic Acetylcholine Receptor

Utkin

Weise

Kasheverov

et al. 2012

Journal of Biological Chemistry

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Background: Venoms from rare snake species may contain toxins of new structural or/and pharmacological types.Results: Amino acid sequence of the new polypeptide azemiopsin isolated from Azemiops feae viper venom was established, and its biological activity was determined.Conclusion: Azemiopsin is the first natural toxin that blocks nicotinic acetylcholine receptors and does not contain disulfide bridges.Significance: Azemiopsin is the first member of a new toxin group.

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Section: Introductionmentioning

confidence: 99%

Azemiopsin from Azemiops feae Viper Venom, a Novel Polypeptide Ligand of Nicotinic Acetylcholine Receptor

Utkin

Weise

Kasheverov

et al. 2012

Journal of Biological Chemistry

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Viper Venom Botox: The Molecular Origin and Evolution of the Waglerin Peptides Used in Anti-Wrinkle Skin Cream

Debono

Xie

Violette³

et al. 2016

J Mol Evol

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The molecular origin of waglerin peptides has remained enigmatic despite their industrial application in skin cream products to paralyse facial muscles and thus reduce the incidence of wrinkles. Here we show that these neurotoxic peptides are the result of de novo evolution within the prepro region of the C-type natriuretic peptide gene in Tropidolaemus venoms, at a site distinct from the domain encoding for the natriuretic peptide. It is the same region that yielded the azemiopsin peptides from Azemiops feae, indicative of a close relationship of this toxin gene between these two genera. The precursor region for the molecular evolution is a biodiversity hotspot that has yielded other novel bioactive peptides with novel activities. We detail the diversity of components in this and other species in order to explore what characteristics enable it to be such a biodiscovery treasure trove. The unusual function of Tropidolaemus venoms may have been selected for due to evolutionary pressures brought about by a high likelihood of prey escape.

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Evolutionary Interpretations of Nicotinic Acetylcholine Receptor Targeting Venom Effects by a Clade of Asian Viperidae Snakes

et al. 2020

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The new peptide from the Fea’s viper Azemiops feae venom interacts with nicotinic acetylcholine receptors

Cited by 4 publications

References 9 publications

Azemiopsin from Azemiops feae Viper Venom, a Novel Polypeptide Ligand of Nicotinic Acetylcholine Receptor

Azemiopsin from Azemiops feae Viper Venom, a Novel Polypeptide Ligand of Nicotinic Acetylcholine Receptor

Viper Venom Botox: The Molecular Origin and Evolution of the Waglerin Peptides Used in Anti-Wrinkle Skin Cream

Evolutionary Interpretations of Nicotinic Acetylcholine Receptor Targeting Venom Effects by a Clade of Asian Viperidae Snakes

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