Isolation and structural identification of a potassium ion channel Kv4.1 inhibitor SsTx-P2 from centipede venom.
10.3724/zdxbyxb-2023-0430
- Author:
Canwei DU
1
;
Fuchu YUAN
2
;
Xinyi DUAN
3
;
Mingqiang RONG
2
;
Er MENG
3
;
Changjun LIU
4
Author Information
1. School of Life and Health Sciences, Hunan University of Science and Technology, Xiangtan 411201, Hunan Province, China. ducw2022@163.com.
2. College of Life Sciences, Hunan Normal University, Changsha 410006, China.
3. School of Life and Health Sciences, Hunan University of Science and Technology, Xiangtan 411201, Hunan Province, China.
4. School of Life and Health Sciences, Hunan University of Science and Technology, Xiangtan 411201, Hunan Province, China. liuchangjun@hnust.edu.cn.
- Publication Type:Journal Article
- Keywords:
Centipede venom;
Inhibitor;
Kv4.1 channel;
Peptide SsTx-P2;
Structure
- From:
Journal of Zhejiang University. Medical sciences
2024;():1-7
- CountryChina
- Language:English
-
Abstract:
OBJECTIVES:To isolate potassium ion channel Kv4.1 inhibitor from centipede venom, and to determine its primary and spatial 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 MALDI-TOF, its primary sequence was determined by Edman degradation sequencing and two-dimensional mass spectrometry, its patial structure was established based on iterative thread assembly refinement online analysis.
RESULTS:A peptide SsTx-P2 was separated from centipede venom with the molecular weight of 6122.8, and its primary sequence consists of 53 amino acid residues, showed as NH2-ELTWDFVRTCCKLFPDKSECTKACATEFTGGDESRLKDVWPRKLRSGDSRLKD-OH. Peptide SsTx-P2 potently inhibited the current of Kv4.1 channel transiently transfected in HEK293 cell, with 1.0 μmol/L SsTx-P2 suppressing 95% current of Kv4.1 channel. Its spatial structure showed that SsTx-P2 shared a conserved helical structure.
CONCLUSIONS:The study has isolated a novel peptide SsTx-P2 from centipede venom, which can potently inhibit the potassium ion channel Kv4.1, and its spatial structure displays a certain degree of conservation.
