ArticleJournal of molecular recognition : JMR2026
Synthesis and Binding Affinity Insights of 2-Phenyl-1H-Benzimidazole Inhibitors Targeting FTO by Spectroscopic Characterization and Molecular Docking.
Article in Journal of molecular recognition : JMR, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
In this work, we designed and synthesized 28 structural analogs of 2-phenyl-1H-benzimidazole. Three of these compounds exhibited stronger binding affinity to FTO, as determined by fluorescence spectroscopy. The results indicate that the binding process is spontaneous and occurs primarily via a static quenching mechanism, driven mainly by hydrogen bonding and van der Waals forces. The interactions of these three lead analogs with FTO were further investigated using UV-visible absorption spectroscopy, circular dichroism spectroscopy, and molecular docking. The docking results are consistent with the thermodynamic data. Among the 28 synthesized derivatives, compounds 7, 8, and 11 exhibited the strongest predicted binding affinities toward FTO and were selected for further spectroscopic and molecular docking studies. In preliminary biological evaluation, compound 7 showed antiproliferative activity against K562 cells with an IC
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