| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10879938 | Toxicon | 2012 | 12 Pages |
Abstract
⺠Heterologous expression and purification of PnTx3-4, a toxin that blocks N-, P/Q-, and R-type voltage-gated calcium channels. ⺠Demonstration that recombinant PnTx3-4 shows biological activity similar to the native peptide using two different assays. ⺠Suggestion that PnTx3-4 adopts a knottin scaffold based on primary sequence analysis. ⺠Circular dichroism analysis showing that the peptide is composed of about 53% turns/unordered, 31% α-helix and 16% β-strand.
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Authors
I.A. Souza, E.A. Cino, W.Y. Choy, M.N. Cordeiro, M. Richardson, C. Chavez-Olortegui, M.V. Gomez, M.A.M. Prado, V.F. Prado,