Assignment of the three disulfide bonds in ShK toxin: A potent potassium channel inhibitor from the sea anemone Stichodactyla helianthus

1995 ◽  
Vol 1 (6) ◽  
pp. 291-297 ◽  
Author(s):  
Jan Pohl ◽  
Frantisek Hubalek ◽  
Michael E. Byrnes ◽  
Kurt R. Nielsen ◽  
Amina Woods ◽  
...  
Keyword(s):  
Potassium Channel ◽  
Disulfide Bonds ◽  
Sea Anemone ◽  
Toxin A

Chemical synthesis and characterization of ShK toxin: a potent potassium channel inhibitor from a sea anemone

2009 ◽  
Vol 46 (5) ◽  
pp. 354-358 ◽  
Author(s):  
M. W. PENNINGTON ◽  
M. E. BYRNES ◽  
I. ZAYDENBERG ◽  
I. KHAYTIN ◽  
J. DE CHASTONAY ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Potassium Channel ◽  
Sea Anemone ◽  
Synthesis And Characterization ◽  
Toxin A

Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone

1996 ◽  
Vol 3 (4) ◽  
pp. 317-320 ◽  
Author(s):  
Jane E. Tudor ◽  
Paul K. Pallaghy ◽  
Michael W. Pennington ◽  
Raymond S. Norton
Keyword(s):  
Potassium Channel ◽  
Solution Structure ◽  
Sea Anemone ◽  
Toxin A

scholarly journals Corrigendum to “Structure, folding and stability of a minimal homologue from Anemonia sulcata of the sea anemone potassium channel blocker ShK” [Peptides 99 (2018) 169–178]

Peptides ◽  
2018 ◽  
Vol 101 ◽  
pp. 234
Author(s):  
Bankala Krishnarjuna ◽  
Christopher A. MacRaild ◽  
Punnepalli Sunanda ◽  
Rodrigo A.V. Morales ◽  
Steve Peigneur ◽  
...  
Keyword(s):  
Potassium Channel ◽  
Channel Blocker ◽  
Sea Anemone ◽  
Potassium Channel Blocker ◽  
Anemonia Sulcata

scholarly journals Sea Anemone Peptides with a Specific Blocking Activity against the Fast Inactivating Potassium Channel Kv3.4

1998 ◽  
Vol 273 (12) ◽  
pp. 6744-6749 ◽  
Author(s):  
Sylvie Diochot ◽  
Hugues Schweitz ◽  
Lászlo Béress ◽  
Michel Lazdunski
Keyword(s):  
Potassium Channel ◽  
Sea Anemone ◽  
Blocking Activity

A potassium channel neurotoxin from the sea anemone Sitchodactyla mertensii (Papua New Guinea)

Toxicon ◽  
1997 ◽  
Vol 35 (6) ◽  
pp. 811
Author(s):  
E. Karlsson ◽  
D. Mebs ◽  
L.C. Young ◽  
A.L. Harvey
Keyword(s):  
Potassium Channel ◽  
Papua New Guinea ◽  
New Guinea ◽  
Sea Anemone

scholarly journals Designer and natural peptide toxin blockers of the KcsA potassium channel identified by phage display

2015 ◽  
Vol 112 (50) ◽  
pp. E7013-E7021 ◽  
Author(s):  
Ruiming Zhao ◽  
Hui Dai ◽  
Netanel Mendelman ◽  
Luis G. Cuello ◽  
Jordan H. Chill ◽  
...  
Keyword(s):  
Phage Display ◽  
Potassium Channel ◽  
Lipid Bilayers ◽  
Disulfide Bonds ◽  
3D Structure ◽  
Structural Basis ◽  
Voltage Sensitivity ◽  
Type I ◽  
High Affinity ◽  
Kv1.3 Channels

Peptide neurotoxins are powerful tools for research, diagnosis, and treatment of disease. Limiting broader use, most receptors lack an identified toxin that binds with high affinity and specificity. This paper describes isolation of toxins for one such orphan target, KcsA, a potassium channel that has been fundamental to delineating the structural basis for ion channel function. A phage-display strategy is presented whereby ∼1.5 million novel and natural peptides are fabricated on the scaffold present in ShK, a sea anemone type I (SAK1) toxin stabilized by three disulfide bonds. We describe two toxins selected by sorting on purified KcsA, one novel (Hui1, 34 residues) and one natural (HmK, 35 residues). Hui1 is potent, blocking single KcsA channels in planar lipid bilayers half-maximally (Ki) at 1 nM. Hui1 is also specific, inhibiting KcsA-Shaker channels in Xenopus oocytes with a Ki of 0.5 nM whereas Shaker, Kv1.2, and Kv1.3 channels are blocked over 200-fold less well. HmK is potent but promiscuous, blocking KcsA-Shaker, Shaker, Kv1.2, and Kv1.3 channels with Ki of 1–4 nM. As anticipated, one Hui1 blocks the KcsA pore and two conserved toxin residues, Lys21 and Tyr22, are essential for high-affinity binding. Unexpectedly, potassium ions traversing the channel from the inside confer voltage sensitivity to the Hui1 off-rate via Arg23, indicating that Lys21 is not in the pore. The 3D structure of Hui1 reveals a SAK1 fold, rationalizes KcsA inhibition, and validates the scaffold-based approach for isolation of high-affinity toxins for orphan receptors.

Characterization of a potassium channel toxin from the Caribbean sea anemone Stichodactyla helianthus

Toxicon ◽  
1995 ◽  
Vol 33 (5) ◽  
pp. 603-613 ◽  
Author(s):  
Olga Castañeda ◽  
Vivian Sotolongo ◽  
Ana Maria Amor ◽  
Reto Stöcklin ◽  
Amanda J. Anderson ◽  
...  
Keyword(s):  
Potassium Channel ◽  
Caribbean Sea ◽  
Sea Anemone ◽  
The Caribbean

scholarly journals APETx4, a Novel Sea Anemone Toxin and a Modulator of the Cancer-Relevant Potassium Channel KV10.1

Marine Drugs ◽  
2017 ◽  
Vol 15 (9) ◽  
pp. 287 ◽  
Author(s):  
Lien Moreels ◽  
Steve Peigneur ◽  
Diogo Galan ◽  
Edwin De Pauw ◽  
Lászlo Béress ◽  
...  
Keyword(s):  
Potassium Channel ◽  
Sea Anemone ◽  
Sea Anemone Toxin
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