{"entity": "researcher", "timestamp": "2026-08-23T09:24:54.237Z", "family": "Wang", "given": "Hao", "initials": "H", "orcid": "0000-0002-1961-0787", "affiliations": ["CAS Center for Excellence in Nanoscience, CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology (NCNST), No. 11 Beiyitiao, Zhongguancun, 100190 Beijing, China.", "Center of Materials Science and Optoelectronics Engineering, University of Chinese Academy of Sciences, No. 19A Yuquan Road, 100049 Beijing, China."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/a24426b63f2a4e1aacc1139d8fa9fb89.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/a24426b63f2a4e1aacc1139d8fa9fb89"}}, "publications": [{"entity": "publication", "iuid": "a59244eb0465478ead3083a353a2bea0", "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"}]}