| Molecular docking study of anethole for anti-breast cancer activity |
| کد مقاله : 1286-ICOC |
| نویسندگان |
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طوبی عبدی زاده * شهرکرد-دانشگاه علوم پزشکی شهرکرد. |
| چکیده مقاله |
| Subject: Breast cancer is one of the most common malignancies among women worldwide [1]. Various genes develop breast cancer risk. The Mammalian Target of Rapamycin (mTOR) is a risk factor mutated in numerous types of breast carcinoma [2]. Anethole, as a natural product, a flavored and major compound extracted from anise, fennel, and licorice, may have anticancer properties [3]. Objective: The study aimed to investigate anethole compound as an mTOR inhibitor in breast cancer treatment. Methods: The 3D-structure of the mTOR protein was obtained from the PDB database and saved in pdb format. Anethole (PubChem CID:637563) was retrieved in sdf format using the PubChem database. Then, molecular docking was carried out between the anethole and the mTOR protein in the active site of the enzyme using Autodock software. Results: Docking analysis demonstrated good binding affinity of anethole to mTOR protein, with a binding energy of -7.65 kcal/mol. Additionally, anethole had appropriate interactions with some of the amino acid residues in the binding site of mTOR, such as Lys121, Asp68, Lys121, and His71. Conclusions: These findings showed that anethole may be able to inhibit the mTOR protein and can be further evaluated by experimental studies. Subject: Breast cancer is one of the most common malignancies among women worldwide [1]. Various genes develop breast cancer risk. The Mammalian Target of Rapamycin (mTOR) is a risk factor mutated in numerous types of breast carcinoma [2]. Anethole, as a natural product, a flavored and major compound extracted from anise, fennel, and licorice, may have anticancer properties [3]. Objective: The study aimed to investigate anethole compound as an mTOR inhibitor in breast cancer treatment. Methods: The 3D-structure of the mTOR protein was obtained from the PDB database and saved in pdb format. Anethole (PubChem CID:637563) was retrieved in sdf format using the PubChem database. Then, molecular docking was carried out between the anethole and the mTOR protein in the active site of the enzyme using Autodock software. Results: Docking analysis demonstrated good binding affinity of anethole to mTOR protein, with a binding energy of -7.65 kcal/mol. Additionally, anethole had appropriate interactions with some of the amino acid residues in the binding site of mTOR, such as Lys121, Asp68, Lys121, and His71. Conclusions: These findings showed that anethole may be able to inhibit the mTOR protein and can be further evaluated by experimental studies. |
| کلیدواژه ها |
| Breast cancer, Anethole, Molecular docking |
| وضعیت: پذیرفته شده |