Snake toxins from mamba venoms: unique tools for the physiologist

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Snake venoms are complex mixtures of small molecules, peptides and proteins. Most of the biologically active toxins are peptides or enzymes. The peptides belong to several structural classes, and they have many different biological actions. The best characterised are the so-called three-finger toxins that have three peptide loops stabilised by four disulphide bridges. Despite their common 3D shape, these peptides can interfere selectively with different biological targets, including nicotinic and muscarinic acetylcholine receptors, acetylcholinesterase, ion channels, and cell membranes. Other small peptides can block K(+) or Ca(2+) channels and are based on Kunitz serine proteinase inhibitors. This article summarises the proteins and peptides isolated from venoms of mamba snakes ( Dendroaspis genus) that have been useful as experimental tools for physiologists and pharmacologists.
LanguageEnglish
Pages689-692
Number of pages4
JournalActa Chimica Slovenica
Volume58
Issue number4
Publication statusPublished - 2011

Fingerprint

Venoms
Peptides
Snake Venoms
Serine Proteinase Inhibitors
Nicotinic Receptors
Muscarinic Receptors
Cell membranes
Acetylcholinesterase
Complex Mixtures
Ion Channels
Disulfides
Proteins
Molecules
Enzymes

Keywords

  • gene organization
  • mamba toxins
  • muscarinic toxins
  • peptide
  • nicotinic acetylcholine-receptors
  • bungarotoxin
  • neurotoxin
  • alpha-7
  • mamba venom
  • natriuretic peptides
  • calciseptine
  • receptor
  • antagonist
  • proteins
  • green mamba
  • ion channel
  • snake toxins
  • physiologist
  • tools

Cite this

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title = "Snake toxins from mamba venoms: unique tools for the physiologist",
abstract = "Snake venoms are complex mixtures of small molecules, peptides and proteins. Most of the biologically active toxins are peptides or enzymes. The peptides belong to several structural classes, and they have many different biological actions. The best characterised are the so-called three-finger toxins that have three peptide loops stabilised by four disulphide bridges. Despite their common 3D shape, these peptides can interfere selectively with different biological targets, including nicotinic and muscarinic acetylcholine receptors, acetylcholinesterase, ion channels, and cell membranes. Other small peptides can block K(+) or Ca(2+) channels and are based on Kunitz serine proteinase inhibitors. This article summarises the proteins and peptides isolated from venoms of mamba snakes ( Dendroaspis genus) that have been useful as experimental tools for physiologists and pharmacologists.",
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Snake toxins from mamba venoms : unique tools for the physiologist. / Rowan, E. G.; Harvey, A. L.

In: Acta Chimica Slovenica, Vol. 58, No. 4, 2011, p. 689-692.

Research output: Contribution to journalArticle

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T1 - Snake toxins from mamba venoms

T2 - Acta Chimica Slovenica

AU - Rowan, E. G.

AU - Harvey, A. L.

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