{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,29]],"date-time":"2026-03-29T10:29:12Z","timestamp":1774780152754,"version":"3.50.1"},"reference-count":43,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2023,2,28]],"date-time":"2023-02-28T00:00:00Z","timestamp":1677542400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"NSERC (Canada)"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JFB"],"abstract":"<jats:p>Microtubules are cylindrical protein polymers assembled in the cytoplasm of all eukaryotic cells by polymerization of a\u03b2 tubulin dimers, which are involved in cell division, migration, signaling, and intracellular traffic. These functions make them essential in the proliferation of cancerous cells and metastases. Tubulin has been the molecular target of many anticancer drugs because of its crucial role in the cell proliferation process. By developing drug resistance, tumor cells severely limit the successful outcomes of cancer chemotherapy. Hence, overcoming drug resistance motivates the design of new anticancer therapeutics. Here, we retrieve short peptides obtained from the data repository of antimicrobial peptides (DRAMP) and report on the computational screening of their predicted tertiary structures for the ability to inhibit tubulin polymerization using multiple combinatorial docking programs, namely PATCHDOCK, FIREDOCK, and ClusPro. The interaction visualizations show that all the best peptides from the docking analysis bind to the interface residues of the tubulin isoforms \u03b1\u03b2l, \u03b1\u03b2ll, \u03b1\u03b2lll, and \u03b1\u03b2lV, respectively. The docking studies were further confirmed by a molecular dynamics simulation, in which the computed root-mean-square deviation (RMSD), and root-mean-square fluctuation (RMSF), verified the stable nature of the peptide\u2013tubulin complexes. Physiochemical toxicity and allergenicity studies were also performed. This present study suggests that these identified anticancer peptide molecules might destabilize the tubulin polymerization process and hence can be suitable candidates for novel drug development. It is concluded that wet-lab experiments are needed to validate these findings.<\/jats:p>","DOI":"10.3390\/jfb14030135","type":"journal-article","created":{"date-parts":[[2023,2,28]],"date-time":"2023-02-28T03:29:46Z","timestamp":1677554986000},"page":"135","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["A Molecular Docking Study Reveals That Short Peptides Induce Conformational Changes in the Structure of Human Tubulin Isotypes \u03b1\u03b2I, \u03b1\u03b2II, \u03b1\u03b2III and \u03b1\u03b2IV"],"prefix":"10.3390","volume":"14","author":[{"given":"Oluwakemi","family":"Ebenezer","sequence":"first","affiliation":[{"name":"Department of Chemistry, Faculty of Natural Science, Mangosuthu University of Technology, Umlazi 4031, South Africa"},{"name":"Department of Biological Sciences, University of Alberta, Edmonton, AB T6G 2E9, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nkululeko","family":"Damoyi","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Natural Science, Mangosuthu University of Technology, Umlazi 4031, South Africa"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael","family":"Shapi","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Faculty of Natural Science, Mangosuthu University of Technology, Umlazi 4031, South Africa"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6108-5560","authenticated-orcid":false,"given":"Gane Ka-Shu","family":"Wong","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, University of Alberta, Edmonton, AB T6G 2E9, Canada"},{"name":"Li Ka Shing Institute of Virology, University of Alberta, Edmonton, AB T6G 2E1, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9976-0429","authenticated-orcid":false,"given":"Jack A.","family":"Tuszynski","sequence":"additional","affiliation":[{"name":"Li Ka Shing Institute of Virology, University of Alberta, Edmonton, AB T6G 2E1, Canada"},{"name":"Department of Physics, University of Alberta, Edmonton, AB T6G 2E1, Canada"},{"name":"Department of Oncology, Cross Cancer Institute, University of Alberta, Edmonton, AB T6G 1Z2, Canada"},{"name":"Department of Mechanical and Aerospace Engineering, (DIMEAS), Politecnico di Torino, 10129 Turin, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2023,2,28]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.canlet.2015.07.030","article-title":"Dietary flavonoid fisetin binds to \u03b2-tubulin and disrupts microtubule dynamics in prostate cancer cells","volume":"367","author":"Mukhtar","year":"2015","journal-title":"Cancer Lett."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Ebenezer, O., Shapi, M., and Tuszynski, J.A. 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