N. A. Orlov, S. A. Yakimov, O. V. Nekrasova, A. V. Feofanov
{"title":"蝎毒重组肽Ce1和Ce4及其与杂交通道KcsA-Kv1的相互作用X (X = 1,3,6)","authors":"N. A. Orlov, S. A. Yakimov, O. V. Nekrasova, A. V. Feofanov","doi":"10.3103/s0096392522020067","DOIUrl":null,"url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>A technique has been developed for obtaining recombinant functionally active peptides Ce1 and Ce4 from the venom of the scorpion <i>Centruroides elegans</i> in the Escherichia <i>coli</i> expression system. The yields of peptides Ce1 and Ce4 were 6.5 and 12 mg per liter of culture, respectively. The properties of the obtained peptides were studied using bioengineered systems based on hybrid channels KcsA-K<sub>v</sub>1.x (x = 1, 3, 6) containing blocker binding sites of the corresponding eukaryotic potassium channels of K<sub>v</sub>1-family. It has been shown that recombinant Ce1 and Ce4 do not exhibit affinity to the binding sites of K<sub>v</sub>1.1 and K<sub>v</sub>1.6 channels up to micromolar concentrations and, like natural peptides, selectively interact with the binding site of the K<sub>v</sub>1.3 channel: the apparent dissociation constants of KcsA-K<sub>v</sub>1.3 complexes with recombinant Ce1 and Ce4 are 50 ± 10 and 200 ± 30 nM (mean ± SEM), respectively.</p>","PeriodicalId":19004,"journal":{"name":"Moscow University Biological Sciences Bulletin","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2022-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Recombinant Peptides Ce1 and Ce4 from the Venom of Scorpion Centruroides elegans and Their Interactions with Hybrid Channels KcsA-Kv1.x (x = 1, 3, 6)\",\"authors\":\"N. A. Orlov, S. A. Yakimov, O. V. Nekrasova, A. V. Feofanov\",\"doi\":\"10.3103/s0096392522020067\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<h3 data-test=\\\"abstract-sub-heading\\\">Abstract</h3><p>A technique has been developed for obtaining recombinant functionally active peptides Ce1 and Ce4 from the venom of the scorpion <i>Centruroides elegans</i> in the Escherichia <i>coli</i> expression system. The yields of peptides Ce1 and Ce4 were 6.5 and 12 mg per liter of culture, respectively. The properties of the obtained peptides were studied using bioengineered systems based on hybrid channels KcsA-K<sub>v</sub>1.x (x = 1, 3, 6) containing blocker binding sites of the corresponding eukaryotic potassium channels of K<sub>v</sub>1-family. It has been shown that recombinant Ce1 and Ce4 do not exhibit affinity to the binding sites of K<sub>v</sub>1.1 and K<sub>v</sub>1.6 channels up to micromolar concentrations and, like natural peptides, selectively interact with the binding site of the K<sub>v</sub>1.3 channel: the apparent dissociation constants of KcsA-K<sub>v</sub>1.3 complexes with recombinant Ce1 and Ce4 are 50 ± 10 and 200 ± 30 nM (mean ± SEM), respectively.</p>\",\"PeriodicalId\":19004,\"journal\":{\"name\":\"Moscow University Biological Sciences Bulletin\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2022-09-06\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Moscow University Biological Sciences Bulletin\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3103/s0096392522020067\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"Agricultural and Biological Sciences\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Moscow University Biological Sciences Bulletin","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3103/s0096392522020067","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"Agricultural and Biological Sciences","Score":null,"Total":0}
Recombinant Peptides Ce1 and Ce4 from the Venom of Scorpion Centruroides elegans and Their Interactions with Hybrid Channels KcsA-Kv1.x (x = 1, 3, 6)
Abstract
A technique has been developed for obtaining recombinant functionally active peptides Ce1 and Ce4 from the venom of the scorpion Centruroides elegans in the Escherichia coli expression system. The yields of peptides Ce1 and Ce4 were 6.5 and 12 mg per liter of culture, respectively. The properties of the obtained peptides were studied using bioengineered systems based on hybrid channels KcsA-Kv1.x (x = 1, 3, 6) containing blocker binding sites of the corresponding eukaryotic potassium channels of Kv1-family. It has been shown that recombinant Ce1 and Ce4 do not exhibit affinity to the binding sites of Kv1.1 and Kv1.6 channels up to micromolar concentrations and, like natural peptides, selectively interact with the binding site of the Kv1.3 channel: the apparent dissociation constants of KcsA-Kv1.3 complexes with recombinant Ce1 and Ce4 are 50 ± 10 and 200 ± 30 nM (mean ± SEM), respectively.
期刊介绍：
Moscow University Biological Sciences Bulletin is forum for research in all important areas of modern biology. It publishes original work on qualitative, analytical and experimental aspects of research. The scope of articles to be considered includes plant biology, zoology, ecology, evolutionary biology, biophysics, genetics, genomics, proteomics, molecular biology, cell biology, biochemistry, endocrinology, immunology, physiology, pharmacology, neuroscience, gerontology, developmental biology, bioinformatics, bioengineering, virology, and microbiology.
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