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LEN binds to the HIV-1 capsid protein (CA) at the phenylalanine-glycine (FG) binding pocket (FGBP), a site for multiple host-factor and antiviral interactions in CA hexamers (CA\n                  <jats:sub>HEX<\/jats:sub>\n                  ). Previously, we generated a chemical library to investigate the FGBP; ZW-1261, a lead compound, exhibits potent antiviral activity and strong inter-subunit interactions within CA\n                  <jats:sub>HEX<\/jats:sub>\n                  . Here, we report the molecular mechanism by which ZW-1261 affects the morphology and integrity of capsid lattice. ZW-1261 alone rapidly induces tubular CA assemblies; simultaneous addition of ZW-1261 with the assembly cofactor inositol hexaphosphate (IP6) forms morphologically distinct tubes. In mature virions, IP6 is required for the assembly of both CA\n                  <jats:sub>HEX<\/jats:sub>\n                  and CA pentamers (CA\n                  <jats:sub>PENT<\/jats:sub>\n                  ). Cryogenic-electron microscopy analysis of\n                  <jats:italic>in vitro<\/jats:italic>\n                  assembled capsid-like particles (CLPs) with IP6 suggests that ZW-1261 leads to the absence of CA\n                  <jats:sub>PENT<\/jats:sub>\n                  and damages the pre-formed conical lattice. To elucidate how this FGBP-targeting antiviral impacts CA\n                  <jats:sub>PENT<\/jats:sub>\n                  , we further solved structures of CA\n                  <jats:sub>PENT<\/jats:sub>\n                  -only icosahedral assemblies (T = 1), formed by reported mutations, that were treated with ZW-1261. We find that ZW-1261 binding in these constrained T = 1 assemblies converts CA\n                  <jats:sub>PENT<\/jats:sub>\n                  to a CA\n                  <jats:sub>HEX<\/jats:sub>\n                  -like conformation. Collectively, this suggests a mechanism by which addition of FGBP-binding inhibitor to native cores leads to the absence of CA\n                  <jats:sub>PENT<\/jats:sub>\n                  , impacting capsid closure and core integrity.\n                <\/jats:p>","DOI":"10.64898\/2026.03.19.712970","type":"posted-content","created":{"date-parts":[[2026,3,21]],"date-time":"2026-03-21T04:50:11Z","timestamp":1774068611000},"source":"Crossref","is-referenced-by-count":0,"title":["Damaging the conical morphology of HIV-1 capsid by targeting the FG-binding pocket and disfavoring pentameric subunits needed for core closure"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6911-2172","authenticated-orcid":false,"given":"William M.","family":"McFadden","sequence":"first","affiliation":[{"name":"Center for ViroScience and Cure, Laboratory of Biochemical Pharmacology, Department of Pediatrics, Emory University School of Medicine, Atlanta, GA, 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USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lei","family":"Wang","sequence":"additional","affiliation":[{"name":"Center for Drug Design, College of Pharmacy, University of Minnesota, Minneapolis, MN, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4029-0113","authenticated-orcid":false,"given":"Carolyn M.","family":"Highland","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY, USA"},{"name":"Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0763-8173","authenticated-orcid":false,"given":"Sophie R.","family":"Harvey","sequence":"additional","affiliation":[{"name":"Campus Chemical Instrumentation Center Mass Spectrometry and Proteomics Facility, The Ohio State University, Columbus, OH, USA"},{"name":"Native Mass Spectrometry Guided Structural Biology Center, The Ohio State University, Columbus, OH, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9267-500X","authenticated-orcid":false,"given":"Savannah","family":"Brancato","sequence":"additional","affiliation":[{"name":"Center for ViroScience and Cure, Laboratory of Biochemical Pharmacology, Department of Pediatrics, Emory University School of Medicine, Atlanta, GA, USA"},{"name":"Children\u2019s Healthcare of Atlanta, Atlanta, GA, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0005-1275-9684","authenticated-orcid":false,"given":"Andres","family":"Emanuelli Castaner","sequence":"additional","affiliation":[{"name":"Center for ViroScience and Cure, Laboratory of Biochemical Pharmacology, Department of Pediatrics, Emory University School of Medicine, Atlanta, GA, USA"},{"name":"Children\u2019s Healthcare of Atlanta, Atlanta, GA, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Haijuan","family":"Du","sequence":"additional","affiliation":[{"name":"Center for ViroScience and Cure, Laboratory of Biochemical Pharmacology, Department of Pediatrics, Emory University School of Medicine, Atlanta, GA, USA"},{"name":"Children\u2019s Healthcare of Atlanta, Atlanta, GA, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0495-2538","authenticated-orcid":false,"given":"Vicki H.","family":"Wysocki","sequence":"additional","affiliation":[{"name":"School of Chemistry & Biochemistry, Georgia Institute of Technology, Atlanta, GA, USA"},{"name":"Native MS Guided Structural Biology Center, Georgia Institute of Technology, Atlanta, GA, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1326-5986","authenticated-orcid":false,"given":"Zhengqiang","family":"Wang","sequence":"additional","affiliation":[{"name":"Center 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