Isolation and structural identification of a potassium ion channel Kv4.1 inhibitor SsTx-P2 from centipede venom. / èè£æ¯æ¶²ä¸é¾ç¦»åééKv4.1æå¶åSsTx-P2çå离åç»æé´å®.
Zhejiang Da Xue Xue Bao Yi Xue Ban
; 53(2): 194-200, 2024 Apr 25.
Article
em En, Zh
| MEDLINE
| ID: mdl-38268403
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 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-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 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 displays structural conservation.Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Venenos de Artrópodes
/
Sequência de Aminoácidos
/
Canais de Potássio Shal
Tipo de estudo:
Diagnostic_studies
Limite:
Animals
/
Humans
Idioma:
En
/
Zh
Revista:
Zhejiang Da Xue Xue Bao Yi Xue Ban
Assunto da revista:
MEDICINA
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
China