ArticleScientific reports2026
Quantitative correlation of spectroscopic signatures with ligand-protein interactions in anti-cancer drug Afinitor: an integrated experimental-computational study.
Article in Scientific reports, 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
A detailed molecular-level understanding of anticancer drugs is essential for improving therapeutic efficacy and guiding rational drug design. Everolimus (Afinitor), a clinically important inhibitor of the mammalian target of rapamycin (mTOR) pathway, is widely used in cancer therapy; however, a quantitatively grounded relationship between its spectroscopic characteristics and ligand-protein interactions remains insufficiently explored. In this study, an integrated experimental-computational approach was employed, combining FT-IR spectroscopy, UV-Vis spectroscopy, and molecular docking simulations. Spectroscopic analyses were used to characterise functional groups and electronic structure, while docking simulations were performed to investigate interactions with FK506 binding protein (FKBP12) and the FKBP-rapamycin binding (FRB) domain. FT-IR analysis revealed a high density of oxygen-containing functional groups, including hydroxyl and carbonyl moieties, with vibrational frequencies indicative of a strongly polarised electronic environment. Molecular docking demonstrated favourable binding affinities with FKBP12 (- 9.7 and - 9.6 kcal·mol⁻
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