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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Chen, Jing Zhang, Chuangeng Yang, Weishan Cao, Zhijian Li, Wenxin Chen, Zongyun Wu, Yingliang |
| Description | Country affiliation: China Author Affiliation: Chen J ( Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, Hubei University of Medicine, Hubei, China); Zhang C ( State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Hubei, China.); Yang W ( State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Hubei, China.); Cao Z ( State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Hubei, China.); Li W ( State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Hubei, China.); Chen Z ( Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, Hubei University of Medicine, Hubei, China); Wu Y ( State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Hubei, China. Electronic address: ylwu@whu.edu.cn.) |
| Abstract | Peptides with Ascaris-type fold are a new kind of toxins founded from venomous animals recently. Functionally, these unique toxin peptides had been identified as potent protease inhibitors, which was similar to other known Ascaris-type peptides from non-venomous animals. Whether Ascaris-type peptides from venom animals have neurotoxin activities remains unclear. Here, a scorpion toxin SjAPI-2 with Ascaris-type fold was characterized to have a neurotoxin activity, which can selectively inhibit KCNQ1 potassium channel. SjAPI-2 had 62 amino acid residues, including 10 cysteine residues. Charged residue analyses showed that two acidic residues of SjAPI-2 were regionally distributed, and 10 basic residues were distributed widely throughout the whole peptide, which was similar to classical potassium channel toxins. Pharmacological studies confirmed that SjAPI-2 was a selective KCNQ1 potassium channel inhibitor with weak effects on other potassium channels, such as Kv1.1, Kv1.2, Kv1.3, SKCa2, SKCa3, and IKCa channels. Concentration-dependent studies showed that SjAPI-2 inhibited the KCNQ1 potassium channel with an IC50 of 771.5±169.9 nM. To the best of our knowledge, SjAPI-2 is the first neurotoxin with a unique Ascaris-type fold, providing novel insights into the divergent evolution of neurotoxins from venomous animals. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Volume Number | 79 |
| e-ISSN | 18790003 |
| Journal | International Journal of Biological Macromolecules |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-08-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Arthropod Proteins Chemistry Kcnq1 Potassium Channel Antagonists & Inhibitors Potassium Channel Blockers Scorpion Venoms Amino Acid Sequence Animals Isolation & Purification Pharmacology Base Sequence Cloning, Molecular Hek293 Cells Humans Membrane Potentials Drug Effects Mice Molecular Sequence Data Protein Stability Protein Structure, Secondary Scorpions Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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