2001
DOI: 10.1002/rcm.261
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Conformational study of a new SGTx1 neurotoxin from the spider Scodra griseipes using mass spectrometry

Abstract: SGTx1 is a new neurotoxin from the venom of Scodra griseipes. Because of the small quantity of this natural peptide available, mass spectrometry was used to obtain information on its higher-order structure. The kinetics of reduction by 1,4-dithiothreitol (DTT) was monitored by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS), and showed that one of the three disulfide bridges was appreciably more accessible to the DTT. Studies based on the charge state distribution (CS… Show more

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Cited by 3 publications
(9 citation statements)
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References 45 publications
(82 reference statements)
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“…Thus, we have shown here a dramatic difference in CSD between disulfideintact and disulfide-reduced peptides. Such differences have already been shown for ω-conotoxins 36 and SGTx1 toxin, 37 which contain only 26 and 34 amino acids, respectively. An alternative explanation could involve Coulombic forces at acidic pH in solution.…”
Section: Native α-Dendrotoxinmentioning
confidence: 60%
See 4 more Smart Citations
“…Thus, we have shown here a dramatic difference in CSD between disulfideintact and disulfide-reduced peptides. Such differences have already been shown for ω-conotoxins 36 and SGTx1 toxin, 37 which contain only 26 and 34 amino acids, respectively. An alternative explanation could involve Coulombic forces at acidic pH in solution.…”
Section: Native α-Dendrotoxinmentioning
confidence: 60%
“…Optimization of the parameters was obtained for water + methanol (80 / 20,v : v) at pH 7. 36,37 The ES ionization source temperature was also optimised at 100°C. In fact, at 80°C the spectrum was much too noisy and there was no difference in the CSD, centered at 8+, between these two temperatures.…”
Section: Mass Spectrometry Instrumentationmentioning
confidence: 99%
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