Literature DB >> 6092517

Structural determinants of the affinity of saxitoxin for neuronal sodium channels. Electrophysiological studies on frog peripheral nerve.

G Strichartz.   

Abstract

The potencies of saxitoxin (STX) and of five structurally related toxins were determined by their ability to block impulses at equilibrium in frog sciatic nerve. The order of potency, with values relative to STX potency in parentheses, was: neo-STX (4.5) greater than gonyautoxin (GTX) III (1.4) greater than STX (1.0) greater than GTXII (0.22) greater than 12 alpha-dihydroSTX (0.050) greater than 12 beta-dihydroSTX (0.0014). When equipotent solutions of STX and neo-STX were exchanged, impulses in the treated nerve were transiently overblocked or underblocked, thus kinetically distinguishing neo-STX from STX. Similar phenomena occurred with exchanges of STX and GTXIII. No consistent evidence was found for any blocking activity of STX molecules that were not protonated at the C8 guanidinium, but the pH dependence of STX potency cannot be described simply by the titration of this guanidinium group. The effects of pH and of various substituents on STX potency are accounted for by changes in the molecular forms of STX and by alterations in specific electrical charges on STX and at the receptor. The results support a model in which toxin molecules bind in two steps; initial binding of the C8 guanidinium to an anionic group induces the loss of water from the normally hydrated ketone (at carbon 12), which then forms a weak covalent bond with a nucleophilic group on the receptor.

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Year:  1984        PMID: 6092517      PMCID: PMC2228733          DOI: 10.1085/jgp.84.2.281

Source DB:  PubMed          Journal:  J Gen Physiol        ISSN: 0022-1295            Impact factor:   4.086


  20 in total

1.  Competitive binding interaction between Zn2+ and saxitoxin in cardiac Na+ channels. Evidence for a sulfhydryl group in the Zn2+/saxitoxin binding site.

Authors:  L Schild; E Moczydlowski
Journal:  Biophys J       Date:  1991-03       Impact factor: 4.033

2.  Interactions of neosaxitoxin with the sodium channel of the frog skeletal muscle fiber.

Authors:  S L Hu; C Y Kao
Journal:  J Gen Physiol       Date:  1991-03       Impact factor: 4.086

3.  Discrimination of muscle and neuronal Na-channel subtypes by binding competition between [3H]saxitoxin and mu-conotoxins.

Authors:  E Moczydlowski; B M Olivera; W R Gray; G R Strichartz
Journal:  Proc Natl Acad Sci U S A       Date:  1986-07       Impact factor: 11.205

4.  Specific neosaxitoxin interactions with the Na+ channel outer vestibule determined by mutant cycle analysis.

Authors:  J L Penzotti; G Lipkind; H A Fozzard; S C Dudley
Journal:  Biophys J       Date:  2001-02       Impact factor: 4.033

5.  Differences in saxitoxin and tetrodotoxin binding revealed by mutagenesis of the Na+ channel outer vestibule.

Authors:  J L Penzotti; H A Fozzard; G M Lipkind; S C Dudley
Journal:  Biophys J       Date:  1998-12       Impact factor: 4.033

Review 6.  On the chemistry, toxicology and genetics of the cyanobacterial toxins, microcystin, nodularin, saxitoxin and cylindrospermopsin.

Authors:  Leanne Pearson; Troco Mihali; Michelle Moffitt; Ralf Kellmann; Brett Neilan
Journal:  Mar Drugs       Date:  2010-05-10       Impact factor: 5.118

7.  Marked difference in saxitoxin and tetrodotoxin affinity for the human nociceptive voltage-gated sodium channel (Nav1.7) [corrected].

Authors:  James R Walker; Paul A Novick; William H Parsons; Malcolm McGregor; Jeff Zablocki; Vijay S Pande; J Du Bois
Journal:  Proc Natl Acad Sci U S A       Date:  2012-10-17       Impact factor: 11.205

8.  Cooperativity of tetrodotoxin action in the frog node of Ranvier.

Authors:  E Benoit; J M Dubois
Journal:  Pflugers Arch       Date:  1985-10       Impact factor: 3.657

9.  A mu-conotoxin-insensitive Na+ channel mutant: possible localization of a binding site at the outer vestibule.

Authors:  S C Dudley; H Todt; G Lipkind; H A Fozzard
Journal:  Biophys J       Date:  1995-11       Impact factor: 4.033

10.  Carbodiimide modification reduces the conductance and increases the tetrodotoxin sensitivity in batrachotoxin-modified sodium channels.

Authors:  L D Chabala; O S Andersen
Journal:  Pflugers Arch       Date:  1992-06       Impact factor: 3.657

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