{"entity": "publication", "iuid": "a59244eb0465478ead3083a353a2bea0", "timestamp": "2026-08-23T09:24:52.828Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/a59244eb0465478ead3083a353a2bea0.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/a59244eb0465478ead3083a353a2bea0"}}, "title": "Homologous Peptide Foldamer Promotes FUS Aggregation and Triggers Cancer Cell Death.", "authors": [{"family": "Wang", "given": "Man-Di", "initials": "MD", "orcid": "0009-0002-2464-839X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ec771ce552804a3bb5f5c161d9e5d192.json"}}, {"family": "Yi", "given": "Li", "initials": "L"}, {"family": "Li", "given": "Yanying", "initials": "Y"}, {"family": "Xu", "given": "Ruiwen", "initials": "R"}, {"family": "Hu", "given": "Jiaojiao", "initials": "J"}, {"family": "Hou", "given": "Da-Yong", "initials": "DY", "orcid": "0000-0002-7567-8663", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e0c47f808e444b5b89262a64e8c538db.json"}}, {"family": "Liu", "given": "Cong", "initials": "C", "orcid": "0000-0003-3425-6672", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/45f9a49fe96e4886a8df416d674d0310.json"}}, {"family": "Wang", "given": "Hao", "initials": "H", "orcid": "0000-0002-1961-0787", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a24426b63f2a4e1aacc1139d8fa9fb89.json"}}], "type": "journal article", "published": "2024-10-23", "journal": {"title": "Journal of the American Chemical Society", "issn": "1520-5126", "volume": "146", "issue": "42", "pages": "28669-28676", "issn-l": "0002-7863"}, "abstract": "Fused in sarcoma (FUS), a multifunctional deoxyribonucleic acid (DNA)/ribonucleic acid (RNA)-binding protein, has been implicated in various cancer types, including sarcoma and leukemia. Despite its association with these diseases, there has been limited exploration of FUS as a cancer therapy target, primarily because its dynamic nature makes it difficult to target specifically. In this study, we explored a kind of \u03b2-sheet peptide foldamer, named \u03b24-TAT, to influence FUS aggregation by targeting its RNA recognition motifs (RRM). This approach leverages the noncovalent interaction characteristics of peptide self-assembly processes. The \u03b24 sequence, derived from the FUS RRM \u03b2-sheet, in combination with TAT, a peptide known for its nuclear targeting capability, enables \u03b24-TAT to bind specifically to the analogous \u03b24 sequence within FUS. Notably, \u03b24-TAT effectively induces FUS aggregation within cells, leading to the death of cancer cells. Our work developed a novel peptide foldamer-based strategy for inducing protein aggregation, paving the way for innovative therapeutic approaches in targeting FUS-associated cancers.", "doi": "10.1021/jacs.4c03420", "pmid": "39403745", "labels": [], "xrefs": [], "notes": [], "created": "2026-08-21T11:38:03.771Z", "modified": "2026-08-21T11:38:03.963Z"}