Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

New ShK-Like Peptide from the Jellyfish Nemopilema nomurai Has Human Potassium Voltage-Gated Channel-Blocking Activity

Version 1 : Received: 18 September 2023 / Approved: 19 September 2023 / Online: 19 September 2023 (08:18:20 CEST)

How to cite: Kim, Y.-J.; Jo, Y.; Lee, S. E.; Kim, J.; Choi, J.-P.; Lee, N.; Won, H.; Woo, D. H.; Yum, S. New ShK-Like Peptide from the Jellyfish Nemopilema nomurai Has Human Potassium Voltage-Gated Channel-Blocking Activity. Preprints 2023, 2023091253. https://doi.org/10.20944/preprints202309.1253.v1 Kim, Y.-J.; Jo, Y.; Lee, S. E.; Kim, J.; Choi, J.-P.; Lee, N.; Won, H.; Woo, D. H.; Yum, S. New ShK-Like Peptide from the Jellyfish Nemopilema nomurai Has Human Potassium Voltage-Gated Channel-Blocking Activity. Preprints 2023, 2023091253. https://doi.org/10.20944/preprints202309.1253.v1

Abstract

We have identified a new human voltage-gated potassium channel (hKv1.3) blocker, NnK-1, in the jellyfish Nemopilema nomurai, based on its genomic information. The gene sequence encoding NnK-1 contains 5,408 base pairs, with five introns and six exons. The coding sequence of the NnK-1 precursor is 894 nucleotides long and encodes 297 amino acids, containing five presumptive ShK-like peptides. An electrophysiological assay demonstrated that the chemically synthesized fifth peptide, NnK-1, is an effective hKv1.3 blocker. A multiple sequence alignment with cnidarian Shk-like peptides, which have Kv1.3-blocking activity, revealed that four residues (3Asp, 25Lys, 33Lys, and 34Thr) of NnK-1, together with six cysteine residues, are conserved. Therefore, we hypothesize that these four residues are crucial for the binding of the toxins to voltage-gated potassium channels.

Keywords

toxin; venom; jellyfish; Cnidaria; genomic information; electrophysiology

Subject

Biology and Life Sciences, Neuroscience and Neurology

Comments (0)

We encourage comments and feedback from a broad range of readers. See criteria for comments and our Diversity statement.

Leave a public comment
Send a private comment to the author(s)
* All users must log in before leaving a comment
Views 0
Downloads 0
Comments 0
Metrics 0


×
Alerts
Notify me about updates to this article or when a peer-reviewed version is published.
We use cookies on our website to ensure you get the best experience.
Read more about our cookies here.