The Role of Disulfide Bond Replacements in Analogues of the Tarantula Toxin ProTx-II and Their Effects on Inhibition of the Voltage-Gated Sodium Ion Channel Na(v)1.7

[Image: see text] Spider venom toxins, such as Protoxin-II (ProTx-II), have recently received much attention as selective Na(v)1.7 channel blockers, with potential to be developed as leads for the treatment of chronic nocioceptive pain. ProTx-II is a 30-amino acid peptide with three disulfide bonds...

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Bibliographic Details
Published in:	J Am Chem Soc
Main Authors:	Wright, Zoë V. F., McCarthy, Stephen, Dickman, Rachael, Reyes, Francis E., Sanchez-Martinez, Silvia, Cryar, Adam, Kilford, Ian, Hall, Adrian, Takle, Andrew K., Topf, Maya, Gonen, Tamir, Thalassinos, Konstantinos, Tabor, Alethea B.
Format:	Artigo
Language:	Inglês
Published:	American Chemical Society 2017
Online Access:	https://ncbi.nlm.nih.gov/pmc/articles/PMC5618157/ https://ncbi.nlm.nih.gov/pubmed/28880078 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jacs.7b06506
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The Role of Disulfide Bond Replacements in Analogues of the Tarantula Toxin ProTx-II and Their Effects on Inhibition of the Voltage-Gated Sodium Ion Channel Na(v)1.7

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