| Autor: |
Primak, A. L., Skutel, M. A., Nekrasova, O. V., Arseniev, A. S., Kirpichnikov, M. P., Feofanov, A. V. |
| Předmět: |
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| Zdroj: |
Russian Journal of Bioorganic Chemistry; 2020, Vol. 46 Issue 6, p1011-1017, 7p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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