Natural Anthraquinones as Potential Akt1-Targeted Anticancer Agents

Background: The phosphoinositide 3-kinase/protein kinase B (Akt)/mammalian target of the rapamycin signaling pathway is crucial in cancer progression. Akt1, a vital pathway component, has emerged as a promising therapeutic target. Objectives: This study used molecular docking analysis to investig...

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Main Authors: Shokoofeh Jamshidi, Fatemeh Mahfouzi, Setareh Shojaei, Amir Taherkhani
Format: Article
Language:English
Published: Hamadan University of Medical Sciences 2024-12-01
Series:Avicenna Journal of Medical Biochemistry
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Online Access:https://ajmb.umsha.ac.ir/PDF/ajmb-12-123.pdf
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author Shokoofeh Jamshidi
Fatemeh Mahfouzi
Setareh Shojaei
Amir Taherkhani
author_facet Shokoofeh Jamshidi
Fatemeh Mahfouzi
Setareh Shojaei
Amir Taherkhani
author_sort Shokoofeh Jamshidi
collection DOAJ
description Background: The phosphoinositide 3-kinase/protein kinase B (Akt)/mammalian target of the rapamycin signaling pathway is crucial in cancer progression. Akt1, a vital pathway component, has emerged as a promising therapeutic target. Objectives: This study used molecular docking analysis to investigate the potential of anthraquinones (AQs) as Akt1 inhibitors. Methods: The crystallographic structure of Akt1 was obtained from the Protein Data Bank (PDB ID: 4GV1). Twenty-one AQ compounds were selected for docking analyses using AutoDock 4.0. Binding affinities and interaction modes were compared with two Akt1 reference inhibitors. Results: Eleven AQs demonstrated substantial binding affinity to the Akt1’s catalytic site at nanomolar concentrations. Hypericin and sennidin B exhibited the most potent inhibitory effects, with ΔGbinding values of -11.19 kcal/mol and -10.36 kcal /mol, respectively, surpassing control inhibitors. Hypericin formed three hydrogen bonds and two hydrophobic interactions with the Akt1 catalytic cleft, while sennidin B formed six hydrogen and one hydrophobic interaction. Conclusion: This study identified several AQs, particularly hypericin and sennidin B, as promising Akt1 inhibitors with superior binding affinities compared to reference compounds. These findings provide a foundation for further developing AQ-based Akt1-targeted therapeutics in cancer treatment. Future research should focus on the in vitro and in vivo validation of these compounds’ efficacy and safety profiles.
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spelling doaj-art-e9757247c4fa4dd58ae4c15f43c30f062025-08-20T02:56:06ZengHamadan University of Medical SciencesAvicenna Journal of Medical Biochemistry2345-41132024-12-0112212313010.34172/ajmb.2567Natural Anthraquinones as Potential Akt1-Targeted Anticancer AgentsShokoofeh Jamshidi0https://orcid.org/0000-0002-0646-1882Fatemeh Mahfouzi1https://orcid.org/0009-0005-7939-6048Setareh Shojaei2https://orcid.org/0000-0001-8323-1231Amir Taherkhani 3https://orcid.org/0000-0002-6546-8785Department of Oral and Maxillofacial Pathology, School of Dentistry, Hamadan University of Medical Sciences, Hamadan, IranDepartment of Oral and Maxillofacial Pathology, School of Dentistry, Hamadan University of Medical Sciences, Hamadan, IranDepartment of Oral and Maxillofacial Pathology, School of Dentistry, Hamadan University of Medical Sciences, Hamadan, IranResearch Center for Molecular Medicine, Institute of Cancer, Avicenna Health Research Institute, Hamadan University of Medical Sciences, Hamadan, IranBackground: The phosphoinositide 3-kinase/protein kinase B (Akt)/mammalian target of the rapamycin signaling pathway is crucial in cancer progression. Akt1, a vital pathway component, has emerged as a promising therapeutic target. Objectives: This study used molecular docking analysis to investigate the potential of anthraquinones (AQs) as Akt1 inhibitors. Methods: The crystallographic structure of Akt1 was obtained from the Protein Data Bank (PDB ID: 4GV1). Twenty-one AQ compounds were selected for docking analyses using AutoDock 4.0. Binding affinities and interaction modes were compared with two Akt1 reference inhibitors. Results: Eleven AQs demonstrated substantial binding affinity to the Akt1’s catalytic site at nanomolar concentrations. Hypericin and sennidin B exhibited the most potent inhibitory effects, with ΔGbinding values of -11.19 kcal/mol and -10.36 kcal /mol, respectively, surpassing control inhibitors. Hypericin formed three hydrogen bonds and two hydrophobic interactions with the Akt1 catalytic cleft, while sennidin B formed six hydrogen and one hydrophobic interaction. Conclusion: This study identified several AQs, particularly hypericin and sennidin B, as promising Akt1 inhibitors with superior binding affinities compared to reference compounds. These findings provide a foundation for further developing AQ-based Akt1-targeted therapeutics in cancer treatment. Future research should focus on the in vitro and in vivo validation of these compounds’ efficacy and safety profiles.https://ajmb.umsha.ac.ir/PDF/ajmb-12-123.pdfakt1anthraquinonecancerdrugmolecular dockingtraditional medicine
spellingShingle Shokoofeh Jamshidi
Fatemeh Mahfouzi
Setareh Shojaei
Amir Taherkhani
Natural Anthraquinones as Potential Akt1-Targeted Anticancer Agents
Avicenna Journal of Medical Biochemistry
akt1
anthraquinone
cancer
drug
molecular docking
traditional medicine
title Natural Anthraquinones as Potential Akt1-Targeted Anticancer Agents
title_full Natural Anthraquinones as Potential Akt1-Targeted Anticancer Agents
title_fullStr Natural Anthraquinones as Potential Akt1-Targeted Anticancer Agents
title_full_unstemmed Natural Anthraquinones as Potential Akt1-Targeted Anticancer Agents
title_short Natural Anthraquinones as Potential Akt1-Targeted Anticancer Agents
title_sort natural anthraquinones as potential akt1 targeted anticancer agents
topic akt1
anthraquinone
cancer
drug
molecular docking
traditional medicine
url https://ajmb.umsha.ac.ir/PDF/ajmb-12-123.pdf
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AT setarehshojaei naturalanthraquinonesaspotentialakt1targetedanticanceragents
AT amirtaherkhani naturalanthraquinonesaspotentialakt1targetedanticanceragents