NOXIUSTOXIN 2, A NOVEL K+ CHANNEL BLOCKING PEPTIDE FROM THE VENOM OF THE SCORPION CENTRUROIDES NOXIUS HOFFMANN

摘要

A novel peptide called Noxiustoxin 2 (NTX2) was purified from the venom of the scorpion Centruroides noxius and characterized chemically and functionally. It is composed of 38 amino acid residues linked by three disulfide bridges and its primary structure is 61% identical to that of Noxiustoxin (NTX). It is not toxic to mice (using up to 200 mu g/20 g mouse weight) and crustaceans (up to 30 mu g/g of crayfish), but has a paralysing effect on crickets (30 mu g/g animal), It displaces the binding of [I-125]NTX to rat brain synaptosome membranes with a K-i of 0.1 mu M, in comparison NTX has a K-i of 100 pM, Similarly, using single Ca2+ activated K+ channels of small conductance obtained from cultured bovine aortic endothelial cells it was shown that NTX2 is over two logarithm units less potent than NTX in producing 50% blockade of the probability of opening the channels. NTX2 is not recognized by a panel of six distinct monoclonal antibodies against NTX, however it is recognized by polyclonal antibodies raised in mouse, with native NTX. Primary structure comparison of both NTX and NTX2 suggests that the N-terminal segments of these peptides are important for channel affinity. Copyright (C) 1996 Elsevier Science Ltd [References: 29]