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Please use this identifier to cite or link to this item:
http://hdl.handle.net/1834/2917
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| Title: | Pharmacological characterization of bunodosoma toxins on mammalian voltage dependent sodium channels. |
| Authors: | Garateix, A.
Salceda, E.
López, O.
Salazar, H.
Aneiros, A.
Zaharenko, A. J.
de Freitas, J. C. |
| ASFA Terms: | Sodium |
| Issue Date: | 2006 |
| Citation: | Pharmacologyonline, (3). p. 507-513 |
| Abstract: | Voltage dependent sodium channels represent an important target for
different neurotoxins and there have been identified different binding
sites according to these interactions. The so called site 3 toxins
comprise a diverse group of peptides obtained from sea anemones and
α-scorpions that bind to voltage gated sodium channels slowing down
the inactivation process. These polypeptides vary considerably in their
affinities for the sodium channels in different excitable cells. In this
work we studied the pharmacological action of three toxins: BcIII
(isolated from Bunodosoma caissarum), BgII and BgIII (isolated from
Bunodosoma granulifera) on isolated cultured neurons of rat dorsal
root ganglia. The biophysical effects and the potency of these
polypeptides were compared and their effects were studied using whole
cell patch clamp techniques. These compounds considerably prolonged
the action potential and selectively slowed down the inactivation
process of tetrodotoxin-sensitive (TTX-S) sodium current. The potency
of these compounds according to the IC50 values was of: BcIII 2.7 ± 2
μM, BgII 4.1 ± 1.2 μM and BgIII 11.9 ± 1.4 μM. These differences
could be determined for the slight variations in the amino acid
composition of these peptides and the contribution of specific amino
acids in the binding to the sodium channel. |
| URI: | http://hdl.handle.net/1834/2917 |
| Appears in Collections: | 1. Articulos científicos
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