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The relative contribution of each domain to their different activities remains to be elucidated. Here, we report the recombinant production, solution structure, and antiparasitic activity of Hge36, first identified as a naturally occurring truncated form of a Scorpine\u2010like peptide from the venom of <jats:italic>Hoffmannihadrurus gertschi<\/jats:italic>. We also show that removing the first four residues from Hge36 renders a molecule with enhanced potassium channel\u2010blocking and antiparasitic activities. Our results are important to rationalize the structure\u2010function relationships of a pharmacologically versatile molecular scaffold.<\/jats:p>","DOI":"10.1002\/1873-3468.12255","type":"journal-article","created":{"date-parts":[[2016,6,17]],"date-time":"2016-06-17T13:56:46Z","timestamp":1466171806000},"page":"2286-2296","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":25,"title":["Solution structure and antiparasitic activity of scorpine\u2010like peptides from <i>Hoffmannihadrurus gertschi<\/i>"],"prefix":"10.1002","volume":"590","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5207-0594","authenticated-orcid":false,"given":"David","family":"Flores\u2010Solis","sequence":"first","affiliation":[{"name":"Departamento de Qu\u00edmica de Biomacromol\u00e9culas Instituto de Qu\u00edmica Universidad Nacional Aut\u00f3noma de M\u00e9xico, CU Ciudad de M\u00e9xico 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