Kv1 Potassium Channel Ligands Based on Hongotoxin 1 and Red Fluorescent Protein
| Autor: | Alexey V. Feofanov, A. S. Arseniev, Mikhail P. Kirpichnikov, Oksana V. Nekrasova, M. A. Skutel, A. L. Primak |
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| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
010405 organic chemistry Potassium Organic Chemistry chemistry.chemical_element 01 natural sciences Biochemistry Fluorescence Potassium channel 0104 chemical sciences Green fluorescent protein law.invention 03 medical and health sciences 030104 developmental biology chemistry law Biophysics Recombinant DNA Bioorganic chemistry Channel blocker Binding site |
| Zdroj: | Russian Journal of Bioorganic Chemistry. 46:1011-1017 |
| ISSN: | 1608-330X 1068-1620 |
| Popis: | Recombinant chimeras of hongotoxin 1 (HgTx1) fused through the N - or C-terminus with the red fluorescent protein TagRFP, RFP-HgTx1 and HgTx1-RFP were obtained. The properties of these fluorescent chimeras as ligands of potassium voltage-gated Kv1 channels were studied using bioengineered cell systems based on hybrid channels KcsA-Kv1.x (x = 1, 3, 6). It is shown that HgTx1-RFP and RFP-HgTx1 are high-affinity ligands of the external pore blocker binding sites of the Kv1.x (x = 1, 3) channels, and HgTx1-RFP is superior in activity to RFP-HgTx1. No specific interactions of HgTx1-RFP and RFP-HgTx1 with KcsA-Kv1. 6 were detected. It has been demonstrated that HgTx1-RFP and RFP-HgTx1 can be used in the KcsA-Kv1.x (x = 1, 3)-based cellular systems to search for Kv1.x (x = 1, 3) channel blockers and estimate their affinity. |
| Databáze: | OpenAIRE |
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