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A theoretical insight in interactions of some chemical compounds as mTOR inhibitors

David Ebuka Arthur, Jibrin Noah Akoji, Riadh Sahnoun, Genevieve Okafor, Karimatu Abdullahi, Samira A. Abdullahi, Charles Mgbemena

2021Bulletin of the National Research Centre/Bulletin of the National Research Center17 citationsDOIOpen Access PDF

Abstract

Abstract Background A series of known Food and Drug Administration (FDA) approved anticancer drugs were collected from the literature and docked against mTOR receptor which has been identified in present time as a target for therapeutic anticancer agents. The compounds binding affinity were calculated after minimising the interaction within the binding pockets’ of the mTOR (4JT6) receptor. Results The result shows that PF-04691502 ligand best inhibited mTOR while occupying the Adenosine triphosphate (ATP)-binding site on the receptor. PF-04691502 had the best binding affinity with a reported value of − 39.261 kcal/mol, and a hydrogen bond energy contribution of − 8.326 kcal/mol. Polamid529 is also found to have a good binding affinity of − 36.75 kcal/mol with the receptor, but was less significant than that calculated for the reference or standard inhibitor (X6K) used (− 37.862 kcal/mol). Further analysis revealed that Palomid529 formed a more stable complex with the receptor than torin2 and X6K due to the significant hydrogen bond contributions it adds to its overall binding score. Conclusion PF-04691502 ligand was identified as the best inhibitor due to its high binding affinity for mTOR and should be considered as the best alternative to the reference inhibitor X6K.

Topics & Concepts

Discovery and development of mTOR inhibitorsHydrogen bondLigand (biochemistry)ChemistryReceptorAdenosine triphosphateStereochemistryBinding sitePI3K/AKT/mTOR pathwayPharmacologyBiochemistryBiologyMoleculeSignal transductionOrganic chemistryPI3K/AKT/mTOR signaling in cancerProtein Kinase Regulation and GTPase SignalingEnzyme function and inhibition
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