{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T06:29:04Z","timestamp":1791613744192,"version":"4.3.4"},"reference-count":5,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"3","license":[{"start":{"date-parts":[[2025,7,1]],"date-time":"2025-07-01T00:00:00Z","timestamp":1751328000000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"content-domain":{"domain":["lww.com","ovid.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2025,7]]},"abstract":"<jats:sec>\n                    <jats:title>Background:<\/jats:title>\n                    <jats:p>\n                      The colchicine-binding site on tubulin is of particular interest for new drug development due to its role in microtubule destabilization and potential to overcome resistance to other agents. Tiliroside, a naturally occurring flavonoid glycoside, has demonstrated anticancer potential\n                      <jats:italic toggle=\"yes\">in vitro<\/jats:italic>\n                      , but its interaction with tubulin has not been previously elucidated.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Objective:<\/jats:title>\n                    <jats:p>This study aimed to investigate the binding of tiliroside to the tubulin site of colchicine, in comparison with colchicine.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods:<\/jats:title>\n                    <jats:p>Molecular docking and molecular dynamics (MD) simulations were employed. Induced-fit docking predicted tiliroside binding, and redocking of colchicine was used to validate the docking protocol. MD simulations (100 ns) were conducted for both tubulin\u2013tiliroside and tubulin\u2013colchicine complexes.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results:<\/jats:title>\n                    <jats:p>\n                      Induced-fit docking predicted that tiliroside binds strongly in the colchicine site, with more favorable scoring metrics than colchicine (Glide GScore \u201316.77 vs \u201310.25, and MMGBSA \u0394G\n                      <jats:sub>bind<\/jats:sub>\n                      \u201350.46 vs \u201336.62 kcal\/mol). Redocking of colchicine reproduced the binding pose (root-mean-square deviation (RMSD) ~0.6 \u00c5). MD simulations further revealed that tiliroside forms a stable complex, remaining securely bound in the pocket. Tiliroside maintained multiple hydrogen bonds and hydrophobic contacts with tubulin, similar to or more persistent than those of colchicine.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion:<\/jats:title>\n                    <jats:p>These results suggest that tiliroside can stably and snugly occupy the colchicine site of tubulin. In summary, our computational study provides structural and dynamic evidence that tiliroside is a high-affinity ligand for the colchicine site, supporting its potential as a lead compound for developing new tubulin-targeted anticancer agents.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.4103\/jpbs.jpbs_1414_25","type":"journal-article","created":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T16:01:26Z","timestamp":1761753686000},"page":"158-165","update-policy":"https:\/\/doi.org\/10.1097\/lww.0000000000001000","source":"Crossref","is-referenced-by-count":8,"title":["Molecular Docking and Dynamics Simulation Reveal Stable Binding of Tiliroside in the Colchicine Site of Tubulin"],"prefix":"10.4103","volume":"17","author":[{"given":"Hani Z.","family":"Asfour","sequence":"first","affiliation":[{"name":"Department of Clinical Microbiology and Immunology, Faculty of Medicine, King Abdulaziz University, Jeddah, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hagar M.","family":"Mohamed","sequence":"additional","affiliation":[{"name":"Department of Medical Laboratory Analysis, College of Medical & Health Sciences, Liwa University, Abu Dhabi, United Arab of Emirates"},{"name":"Department of Applied Medical Chemistry, Medical Research Institute, Alexandria University, Alexandria, Egypt"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abdelsattar M.","family":"Omar","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry, Faculty of Pharmacy, King Abdulaziz University, Jeddah, Saudi Arabia"},{"name":"King Fahd Medical Research Center (KFMRC), King Abdulaziz University (KAU), Jeddah, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nabil A.","family":"Alhakamy","sequence":"additional","affiliation":[{"name":"Center of Excellence for Drug Research and Pharmaceutical Industries, King Abdulaziz University, Jeddah, Saudi Arabia"},{"name":"Department of Pharmaceutics, Faculty of Pharmacy, King Abdulaziz University, Jeddah, Saudi Arabia"},{"name":"Mohamed Saeed Tamer Chair for Pharmaceutical Industries, King Abdulaziz University, Jeddah, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gamal A.","family":"Mohamed","sequence":"additional","affiliation":[{"name":"Department of Natural Products and Alternative Medicine, Faculty of Pharmacy, King Abdulaziz University, Jeddah, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dina S.","family":"El-Agamy","sequence":"additional","affiliation":[{"name":"Department of Pharmacology and Toxicology, Faculty of Pharmacy, Mansoura University, Mansoura, Egypt"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sabrin R.M.","family":"Ibrahim","sequence":"additional","affiliation":[{"name":"Preparatory Year Program, Department of Chemistry, Batterjee Medical College, Jeddah, Saudi Arabia"},{"name":"Department of Pharmacognosy, Faculty of Pharmacy, Assiut University, Assiut, Egypt"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"276","published-online":{"date-parts":[[2025,10,29]]},"reference":[{"key":"R1-20260420","doi-asserted-by":"crossref","first-page":"8","DOI":"10.3390\/ph13010008","article-title":"Colchicine-binding site inhibitors from chemistry to clinic: A review","volume":"13","author":"McLoughlin","year":"2020","journal-title":"Pharmaceuticals"},{"key":"R2-20260420","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12935-022-02786-6","article-title":"Tiliroside suppresses triple-negative breast cancer as a multifunctional CAXII inhibitor","volume":"22","author":"Han","year":"2022","journal-title":"Cancer Cell Int"},{"key":"R3-20260420","doi-asserted-by":"crossref","first-page":"12049","DOI":"10.1021\/acs.jmedchem.1c00715","article-title":"Design, synthesis, and biological evaluation of stable colchicine-binding site tubulin inhibitors 6-aryl-2-benzoyl-pyridines as potential anticancer agents","volume":"64","author":"Chen","year":"2021","journal-title":"J Med Chem"},{"key":"R4-20260420","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1016\/j.drudis.2021.12.001","article-title":"Molecular interactions at the colchicine-binding site in tubulin: An X-ray crystallography perspective","volume":"27","author":"Wang","year":"2022","journal-title":"Drug Discov Today"},{"key":"R5-20260420","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1038\/nature02393","article-title":"Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain","volume":"428","author":"Ravelli","year":"2004","journal-title":"Nature"}],"container-title":["Journal of Pharmacy and Bioallied Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.ovid.com\/10.4103\/jpbs.jpbs_1414_25","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T13:25:56Z","timestamp":1787837156000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.ovid.com\/10.4103\/jpbs.jpbs_1414_25"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,7]]},"references-count":5,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2025]]}},"URL":"https:\/\/doi.org\/10.4103\/jpbs.jpbs_1414_25","relation":{},"ISSN":["0976-4879","0975-7406"],"issn-type":[{"value":"0976-4879","type":"print"},{"value":"0975-7406","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,7]]},"assertion":[{"value":"2025-08-08","name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2025-09-06","name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}}]}}