Conformational study of a new SGTx1 neurotoxin from the spider Scodra griseipes using mass spectrometry

Rapid Communications in Mass Spectrometry : RCM
L Marvin, C Lange

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 (CSD) and H/D exchange of the non-reduced peptide, under neutral and acidic conditions, were performed using electrospray mass spectrometry (ES-MS). In neutral solution, SGTx1 showed a maximum charge state of four compared with seven potentially protonated basic residues, and all labile hydrogens were exchanged. However, under acidic conditions, a maximum charge state of only five was observed, and four of the labile hydrogens could not be deuterated. These observations are interpreted in terms of a rigid structure maintained by the disulfide bridges, which can be temporarily relaxed by disulfide bridge scrambling only at higher pH values.

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Citations

Feb 16, 2011·Proceedings of the National Academy of Sciences of the United States of America·George A PunkosdyEthan M Shevach
Aug 28, 2001·Journal of Mass Spectrometry : JMS

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