Isolation and structural identification of a potassium ion channel Kv4.1 inhibitor SsTx-P2 from centipede venom
10.3724/zdxbyxb-2023-0430
- VernacularTitle:蜈蚣毒液中钾离子通道Kv4.1抑制剂SsTx-P2的分离和结构鉴定
- Author:
Canwei DU
1
;
Fuchu YUAN
;
Xinyi DUAN
;
Mingqiang RONG
;
Er MENG
;
Changjun LIU
Author Information
1. 湖南科技大学生命科学与健康学院,湖南 湘潭 411201
- Keywords:
Centipede;
Peptide;
Potassium channel;
Kv4.1 channel inhibitor;
Structure
- From:
Journal of Zhejiang University. Medical sciences
2024;53(2):194-200
- CountryChina
- Language:Chinese
-
Abstract:
Objective: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 SsTx-P2 was separated from centipede venom with the molecular weight of 6122.8,and its primary sequence consists of 53 amino acid residues NH2-ELTWDFVRTCCKLFPDKSECTKACATEFTGGDESRLKDVWPRKLRSG DSRLKD-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 structure showed that SsTx-P2 shared a conserved helical structure.Conclusion:The study has isolated a novel peptide SsTx-P2 from centipede venom,which can potently inhibit the potassium ion channel Kv4.1 and displays structural conservation.
