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In this study, eight peptide toxins from three distinct spider venom Nav channel families demonstrated robust inhibition of hNav1.7, rKv4.2, and rKv4.3 (rKv4.2\/4.3) currents, exhibiting a similar mode of action. The analysis of structure and function relationship revealed a significant overlap in the pharmacophore responsible for inhibiting hNav1.7 and rKv4.2 by HNTX\u2010III, although Lys25 seems to play a more pivotal role in the inhibition of rKv4.2\/4.3. Pharmacophore\u2010guided rational design is employed for the development of an mGpTx1 analogue, mGpTx1\u2010SA, which retains its inhibition of hNav1.7 while significantly reducing its inhibition of rKv4.2\/4.3 and eliminating cardiotoxicity. Moreover, mGpTx1\u2010SA demonstrates potent analgesic effects in both inflammatory and neuropathic pain models, accompanied by an improved in vivo safety profile. The results suggest that off\u2010target inhibition of rKv4.2\/4.3 by specific spider peptide toxins targeting hNav1.7 may arise from a conserved binding motif. This insight promises to facilitate the design of hNav1.7\u2010specific analgesics, aimed at minimizing rKv4.2\/4.3 inhibition and associated toxicity, thereby enhancing their suitability for therapeutic applications.<\/jats:p>","DOI":"10.1002\/advs.202406656","type":"journal-article","created":{"date-parts":[[2024,9,9]],"date-time":"2024-09-09T07:50:03Z","timestamp":1725868203000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Optimizing Nav1.7\u2010Targeted Analgesics: Revealing Off\u2010Target Effects of Spider Venom\u2010Derived Peptide Toxins and Engineering Strategies for Improvement"],"prefix":"10.1002","volume":"11","author":[{"given":"Sen","family":"Luo","sequence":"first","affiliation":[{"name":"The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development College of Life Sciences Hunan Normal University  Changsha 410081 China"},{"name":"Peptide and small molecule drug R&amp;D 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