Isolation and structural identification of a potassium ion channel Kv4.1 inhibitor SsTx-P2 from centipede venom.

ABSTRACT:

Objectives

To isolate a potassium ion channel Kv4.1 inhibitor from centipede venom, and to determine its sequence and structure.

Methods

Ion-exchange chromatography and reversed-phase high-performance liquid chromatography were performed to separate and purify peptide components of centipede venom, and their inhibiting effect on Kv4.1 channel was determined by whole-cell patch clamp recording. The molecular weight of isolated peptide Kv4.1 channel inhibitor was identified with matrix assisted laser desorption ionization-time-of-flight mass spectrometry; its primary sequence was determined by Edman degradation sequencing and two-dimensional mass spectrometry; its structure was established based on iterative thread assembly refinement online analysis.

Results

A peptide

SUBMITTER: DU C 

PROVIDER: S-EPMC11057981 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature