{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kuzmenkov AI"],"funding":["KU Leuven","Fonds Wetenschappelijk Onderzoek","Russian Science Foundation","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["977440"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9523135"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13"],"pubmed_abstract":["Apamin is often cited as one of the few substances selectively acting on small-conductance Ca<sup>2+</sup>-activated potassium channels (K<sub>Ca</sub>2). However, published pharmacological and structural data remain controversial. Here, we investigated the molecular pharmacology of apamin by two-electrode voltage-clamp in <i>Xenopus laevis</i> oocytes and patch-clamp in HEK293, COS7, and CHO cells expressing the studied ion channels, as well as in isolated rat brain neurons. The microtitre broth dilution method was used for antimicrobial activity screening. The spatial structure of apamin in aqueous solution was determined by NMR spectroscopy. We tested apamin against 42 ion channels (K<sub>Ca</sub>, K<sub>V</sub>, Na<sub>V</sub>, nAChR, ASIC, and others) and confirmed its unique selectiv"],"journal":["Frontiers in pharmacology"],"pubmed_title":["Apamin structure and pharmacology revisited."],"pmcid":["PMC9523135"],"funding_grant_id":["T32GM099608","GOE7120N GOC2319N GOA4919N 12W7822N","T32 GM099608","PDM/19/164"],"pubmed_authors":["Wulff H","Peigneur S","Nikolaev MV","Tytgat J","Vassilevski AA","Mineev KS","Arseniev AS","Nasburg JA","Kuzmenkov AI","Pinheiro-Junior EL"],"additional_accession":[]},"is_claimable":false,"name":"Apamin structure and pharmacology revisited.","description":"Apamin is often cited as one of the few substances selectively acting on small-conductance Ca<sup>2+</sup>-activated potassium channels (K<sub>Ca</sub>2). However, published pharmacological and structural data remain controversial. Here, we investigated the molecular pharmacology of apamin by two-electrode voltage-clamp in <i>Xenopus laevis</i> oocytes and patch-clamp in HEK293, COS7, and CHO cells expressing the studied ion channels, as well as in isolated rat brain neurons. The microtitre broth dilution method was used for antimicrobial activity screening. The spatial structure of apamin in aqueous solution was determined by NMR spectroscopy. We tested apamin against 42 ion channels (K<sub>Ca</sub>, K<sub>V</sub>, Na<sub>V</sub>, nAChR, ASIC, and others) and confirmed its unique selectiv","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2026-06-01T02:23:56.493Z","creation":"2025-04-05T22:22:46.691Z"},"accession":"S-EPMC9523135","cross_references":{"pubmed":["36188602"],"doi":["10.3389/fphar.2022.977440"]}}