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Cell-penetrating peptides (CPPs) can enhance intracellular delivery of PMOs, yet conventional arginine-rich CPPs often cause dose-limiting toxicity, including renal damage, which hinders their clinical translation. To address this challenge, we developed a high-throughput, charge-based chromatographic enrichment platform capable of screening over 15,000 synthetic peptides, including sequences with noncanonical (abiotic) amino acids. This approach enabled de novo discovery of arginine-depleted CPPs with improved delivery profiles. Four lead candidates demonstrated efficient nuclear PMO delivery with ~10-fold lower in vitro toxicity compared to standard CPPs such as penetratin. The top-performing peptide, CXP1, showed robust splice-switching activity and favorable tolerability in both cellular and animal models. In dystrophic mdx mice, CXP1\u2013PMO conjugates achieved greater exon skipping compared to PMOs conjugated to R6G at equivalent doses. Tissue levels of CXP1\u2013PMO correlated with exon-skipping efficacy, establishing a clear pharmacokinetic\u2013pharmacodynamic relationship. These findings highlight a mechanistically novel and translationally relevant discovery strategy, demonstrating the potential of high-throughput platforms to generate more effective CPP-based delivery vehicles for antisense therapeutics in DMD and related neuromuscular disorders.<\/jats:p>\n                <jats:p>\n                  <jats:fig id=\"ufig1\" position=\"float\" fig-type=\"figure\" orientation=\"portrait\">\n                    <jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"730741v1_ufig1\" position=\"float\" orientation=\"portrait\"\/>\n                  <\/jats:fig>\n                <\/jats:p>","DOI":"10.64898\/2026.06.07.730741","type":"posted-content","created":{"date-parts":[[2026,6,11]],"date-time":"2026-06-11T08:30:23Z","timestamp":1781166623000},"source":"Crossref","is-referenced-by-count":1,"title":["High-throughput discovery of arginine-depleted peptides enables effective antisense delivery for Duchenne muscular dystrophy"],"prefix":"10.64898","author":[{"given":"Charlotte E.","family":"Farquhar","sequence":"first","affiliation":[{"name":"Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nathan W.","family":"Dow","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carly K.","family":"Schissel","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anirban","family":"Bardhan","sequence":"additional","affiliation":[{"name":"Sarepta Therapeutics, 215 First Street, Cambridge, MA 02142, 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