scholarly journals Voltage-Gated Potassium Ion Channel Activation

2020 ◽  
Author(s):  
Keyword(s):  
Ion Channel ◽  
Potassium Ion ◽  
Potassium Ion Channel ◽  
Channel Activation ◽  
Voltage Gated

The conformational analysis of a synthetic S4 peptide corresponding to a voltage-gated potassium ion channel protein

FEBS Letters ◽  
1994 ◽  
Vol 349 (3) ◽  
pp. 371-374 ◽  
Author(s):  
Parvez I. Haris ◽  
Bala Ramesh ◽  
Stephen Brazier ◽  
Dennis Chapman
Keyword(s):  
Conformational Analysis ◽  
Ion Channel ◽  
Potassium Ion ◽  
Potassium Ion Channel ◽  
Voltage Gated ◽  
Channel Protein

Voltage-gated potassium ion channel may play a major role in the settlement of Pacific oyster (Crassostrea gigas) larvae

Aquaculture ◽  
2015 ◽  
Vol 442 ◽  
pp. 48-50 ◽  
Author(s):  
Jiao Wang ◽  
Changlu Wu ◽  
Caili Xu ◽  
WenChao Yu ◽  
Zhuang Li ◽  
...  
Keyword(s):  
Ion Channel ◽  
Crassostrea Gigas ◽  
Pacific Oyster ◽  
Potassium Ion ◽  
Potassium Ion Channel ◽  
Voltage Gated

scholarly journals A Novel Insecticidal Spider Peptide that Affects the Mammalian Voltage-Gated Ion Channel hKv1.5

2021 ◽  
Vol 11 ◽  
Author(s):  
Diana Alvarado ◽  
Samuel Cardoso-Arenas ◽  
Ligia-Luz Corrales-García ◽  
Herlinda Clement ◽  
Iván Arenas ◽  
...  
Keyword(s):  
Ion Channel ◽  
Primary Structure ◽  
Potassium Ion ◽  
Potassium Ion Channel ◽  
Mammal Species ◽  
Channel Modulation ◽  
Voltage Gated ◽  
Endoproteolytic Cleavage ◽  
Ion Channel Modulation ◽  
Peptide Toxins

Spider venoms include various peptide toxins that modify the ion currents, mainly of excitable insect cells. Consequently, scientific research on spider venoms has revealed a broad range of peptide toxins with different pharmacological properties, even for mammal species. In this work, thirty animal venoms were screened against hKv1.5, a potential target for atrial fibrillation therapy. The whole venom of the spider Oculicosa supermirabilis, which is also insecticidal to house crickets, caused voltage-gated potassium ion channel modulation in hKv1.5. Therefore, a peptide from the spider O. supermirabilis venom, named Osu1, was identified through HPLC reverse-phase fractionation. Osu1 displayed similar biological properties as the whole venom; so, the primary sequence of Osu1 was elucidated by both of N-terminal degradation and endoproteolytic cleavage. Based on its primary structure, a gene that codifies for Osu1 was constructed de novo from protein to DNA by reverse translation. A recombinant Osu1 was expressed using a pQE30 vector inside the E. coli SHuffle expression system. recombinant Osu1 had voltage-gated potassium ion channel modulation of human hKv1.5, and it was also as insecticidal as the native toxin. Due to its novel primary structure, and hypothesized disulfide pairing motif, Osu1 may represent a new family of spider toxins.

scholarly journals Computational Simulations of Interactions of Scorpion Toxins with the Voltage-Gated Potassium Ion Channel

2004 ◽  
Vol 86 (6) ◽  
pp. 3542-3555 ◽  
Author(s):  
Kunqian Yu ◽  
Wei Fu ◽  
Hong Liu ◽  
Xiaomin Luo ◽  
Kai Xian Chen ◽  
...  
Keyword(s):  
Ion Channel ◽  
Potassium Ion ◽  
Potassium Ion Channel ◽  
Scorpion Toxins ◽  
Computational Simulations ◽  
Voltage Gated

Myrsinane and related diterpenes from Euphorbia falcata with selective potassium ion channel activity

Planta Medica ◽  
2015 ◽  
Vol 81 (16) ◽  
Author(s):  
A Vasas ◽  
P Orvos ◽  
L Tálosi ◽  
P Forgo ◽  
G Pinke ◽  
...  
Keyword(s):  
Ion Channel ◽  
Potassium Ion ◽  
Channel Activity ◽  
Potassium Ion Channel
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