Springer Online Journal Archives 1860-2000
Chemistry and Pharmacology
Abstract This chapter describes biological and pharmacological properties of all peptides from mamba venoms, and relates them to their amino acid sequences classified in two main structural groups. In the first group, which is constituted by peptides homologous to the basic pancreatic trypsin inhibitor (BPTI), there are dendrotoxins, powerful blockers of Kv1 channels with a strong central neurotoxicity; protease inhibitors with weaker activity on K+ channels and calcicludines which are blockers of HVA Ca2+ channels with a potent selective effect on a L-type Ca2+ channel in cerebellar granule neurons. The second group contains all peptides which are structurally homologous to curaremimetic α-neurotoxins: short and long α-neurotoxins; muscarinic toxins which are the unique peptides known to act selectively as agonists or antagonists on one or several of the five muscarinic receptors known; anticholinesterases; ‘angusticeps-type’ peptides with low toxicity and unknown properties; and calciseptines which are specific blockers of L-type Ca2+ channels mainly in the cardiovascular system. In a third group are classified peptides of miscellaneous sizes and structures. The function of most of them has not yet been elucidated. The peculiar interest of the relations between spatial structure and function is illustrated with four peptides from mambas. A method for the purification of all peptides from mamba species is described.
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