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Here, RNA acts as a concentration-dependent regulator of two sequence-related \u03b1-helical peptides with fundamentally different assembly behaviors: the cross-\u03b1 amyloid-forming\n                    <jats:italic>Staphylococcus aureus<\/jats:italic>\n                    virulence factor PSM\u03b13 and the non-amyloidogenic human host-defense peptide LL-37. RNA drives PSM\u03b13 through distinct assembly states, from liquid-like condensates to fibrillar polymorphs, while preserving cytotoxic and antimicrobial activity over time. In contrast, RNA attenuates LL-37 cytotoxicity toward host cells while maintaining antibacterial activity, consistent with a host-protective immunomodulatory effect. Together with the opposing effects of epigallocatechin gallate, which redirects both peptides into amorphous assemblies, these findings support a mechanistic model in which biological activity is governed by supramolecular architecture, assembly trajectory, and dynamics rather than by monomer abundance or mature fibrils alone. More broadly, our findings identify RNA as an environmental regulator of \u03b1-helical peptide assemblies, and establish assembly-state control as a tunable determinant of virulence and host defense.\n                  <\/jats:p>","DOI":"10.7554\/elife.109290","type":"journal-article","created":{"date-parts":[[2026,2,24]],"date-time":"2026-02-24T19:30:14Z","timestamp":1771961414000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.109290","source":"Crossref","is-referenced-by-count":0,"title":["RNA selectively modulates activity of virulent amyloid PSM\u03b13 and host-defense LL-37 via phase separation and aggregation dynamics"],"prefix":"10.7554","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1408-2214","authenticated-orcid":true,"given":"Bader","family":"Rayan","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03qryx823","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biology, Technion - Israel Institute of 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