{"entity": "publication", "iuid": "a455e04b0c6243b6bbabd7b96552b4ac", "timestamp": "2026-08-25T13:27:48.848Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/a455e04b0c6243b6bbabd7b96552b4ac.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/a455e04b0c6243b6bbabd7b96552b4ac"}}, "title": "Single-shot design of a cyclic peptide inhibitor of HIV membrane fusion.", "authors": [{"family": "Daumiller", "given": "Diandra", "initials": "D"}, {"family": "Giammarino", "given": "Federica", "initials": "F"}, {"family": "Li", "given": "Qiuzhen", "initials": "Q"}, {"family": "S\u00f6nnerborg", "given": "Anders", "initials": "A"}, {"family": "Ce\u00f1a Diez", "given": "Rafael", "initials": "R"}, {"family": "Bryant", "given": "Patrick", "initials": "P"}], "type": "journal article", "published": "2026-02-00", "journal": {"title": "Antiviral Res.", "issn": "1872-9096", "volume": "246", "pages": "106336", "issn-l": "0166-3542"}, "abstract": "HIV evades immune detection through rapid mutation of its surface proteins, yet essential steps in viral entry, such as CD4 and co-receptor engagement, remain highly conserved. While therapies like Lenacapavir represent major advances, the emergence of resistant strains highlights the urgent need for adaptable, rapid-response antivirals. This challenge extends beyond HIV, demanding scalable design strategies for diverse viral threats. Here, we demonstrate that AI-driven design can address this need by generating cyclic peptide binders targeting a previously unexploited interface on the HIV-1 fusion protein gp41. Using only sequence information, without prior structural or binding site data, we designed and experimentally validated a single candidate. This inhibitor potently blocked infection by two HIV-1 strains in cell-based assays with no detectable cytotoxicity. Affinity analysis with SPR confirms the interaction with gp41 as designed. Our findings illustrate how AI-guided peptide design, coupled with rapid in-vitro validation, can accelerate early-stage therapeutic discovery and enable timely intervention against emerging viral threats.", "doi": "10.1016/j.antiviral.2025.106336", "pmid": "41423064", "labels": [], "xrefs": [{"db": "pii", "key": "S0166-3542(25)00262-1"}, {"db": "PDB", "key": "3CP1"}, {"db": "PDB", "key": "2R3C"}, {"db": "PDB", "key": "3VH7"}, {"db": "PDB", "key": "3VIE"}, {"db": "PDB", "key": "6TVQ"}], "notes": [], "created": "2026-08-20T06:42:18.489Z", "modified": "2026-08-20T06:42:18.537Z"}