ArticleJournal of pharmacy & bioallied sciences
Molecular Docking and Dynamics Simulation Reveal Stable Binding of Tiliroside in the Colchicine Site of Tubulin.
Article in Journal of pharmacy & bioallied sciences. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Amlodipine besylate, a Dihydropyridine derivative as a Tubulin polymerization inhibitor.Cell biochemistry and biophysics · 2026Article
- Integrated In Silico Prioritization of Antidiabetic Phytochemicals fromMolecules (Basel, Switzerland) · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: 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 Objective: This study aimed to investigate the binding of tiliroside to the tubulin site of colchicine, in comparison with colchicine. Methods: 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-tiliroside and tubulin-colchicine complexes. Results: Induced-fit docking predicted that tiliroside binds strongly in the colchicine site, with more favorable scoring metrics than colchicine (Glide GScore -16.77 vs -10.25, and MMGBSA ΔG Conclusion: 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.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.