Design, eco-friendly synthesis, molecular modeling and anticancer evaluation of thiazol-5(4<i>H</i>)-ones as potential tubulin polymerization inhibitors targeting the colchicine binding site
Abeer M. El‐Naggar, Ibrahim H. Eissa, Amany Belal, Amira A. El‐Sayed
Abstract
value of 9.33 and 9.52 nM, respectively. Further studies revealed the ability of 5a to induce apoptosis and arrest cell cycle growth at the G2/M phase. Molecular docking studies were also conducted to investigate possible binding interactions between the target compounds and the tubulin heterodimer active site. From these studies, it was concluded that inhibition of tubulin polymerization yields the reported cytotoxic activity.
Topics & Concepts
TubulinCytotoxicityChemistryColchicineMTT assayMicrotubule polymerizationMicrotubuleIC50PolymerizationCell cycleCell cycle checkpointDocking (animal)StereochemistryIn vitroBiochemistryPharmacologyApoptosisBiologyCell biologyOrganic chemistryMedicinePolymerNursingGeneticsSynthesis and biological activitySynthesis and Biological EvaluationSynthesis and Characterization of Heterocyclic Compounds