{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,7]],"date-time":"2026-09-07T13:01:55Z","timestamp":1788786115925,"version":"build-2803163510"},"reference-count":77,"publisher":"Wiley","issue":"40","license":[{"start":{"date-parts":[[2024,8,29]],"date-time":"2024-08-29T00:00:00Z","timestamp":1724889600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["advanced.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Advanced Science"],"published-print":{"date-parts":[[2024,10]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Genetic studies have identified the voltage\u2010gated sodium channel 1.7 (\n                    <jats:bold>Na<\/jats:bold>\n                    <jats:sub>\n                      <jats:bold>v<\/jats:bold>\n                    <\/jats:sub>\n                    <jats:bold>1.7<\/jats:bold>\n                    ) as pain target. Due to the ineffectiveness of small molecules and monoclonal antibodies as therapeutics for pain, single\u2010domain antibodies (\n                    <jats:bold>V<\/jats:bold>\n                    <jats:sub>\n                      <jats:bold>H<\/jats:bold>\n                    <\/jats:sub>\n                    <jats:bold>Hs<\/jats:bold>\n                    ) are developed against the human Na\n                    <jats:sub>v<\/jats:sub>\n                    1.7 (\n                    <jats:bold>\n                      hNa\n                      <jats:sub>v<\/jats:sub>\n                      1.7\n                    <\/jats:bold>\n                    ) using a novel antigen presentation strategy. A 70 amino\u2010acid peptide from the hNa\n                    <jats:sub>v<\/jats:sub>\n                    1.7 protein is identified as a target antigen. A recombinant version of this peptide is grafted into the complementarity determining region 3 (\n                    <jats:bold>CDR3<\/jats:bold>\n                    ) loop of an inert V\n                    <jats:sub>H<\/jats:sub>\n                    H in order to maintain the native 3D conformation of the peptide. This antigen is used to isolate one V\n                    <jats:sub>H<\/jats:sub>\n                    H able to i) bind hNa\n                    <jats:sub>v<\/jats:sub>\n                    1.7, ii) slow the deactivation of hNa\n                    <jats:sub>v<\/jats:sub>\n                    1.7, iii) reduce the ability of eliciting action potentials in nociceptors, and iv) reverse hyperalgesia in in vivo rat and mouse models. This V\n                    <jats:sub>H<\/jats:sub>\n                    H exhibits the potential to be developed as a therapeutic capable of suppressing pain. This novel antigen presentation strategy can be applied to develop biologics against other difficult targets such as ion channels, transporters and GPCRs.\n                  <\/jats:p>","DOI":"10.1002\/advs.202405432","type":"journal-article","created":{"date-parts":[[2024,8,29]],"date-time":"2024-08-29T07:04:43Z","timestamp":1724915083000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["A Novel Antigen Design Strategy to Isolate Single\u2010Domain Antibodies that Target Human Nav1.7 and Reduce Pain in Animal Models"],"prefix":"10.1002","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0009-0008-9732-6483","authenticated-orcid":false,"given":"Marzia","family":"Martina","sequence":"first","affiliation":[{"name":"Human Health Therapeutics Research Center National Research Council Canada  1200 Montreal Road, Building M54 Ottawa ON K1A 0R6 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