Akademik Veri Yönetim Sistemi
CUMHURIYET 8th INTERNATIONAL CONFERENCE ON APPLIED SCIENCES, Ankara, Türkiye, 23 Nisan 2023, ss.13
Breast cancer is more common in women around the world and has a high malignancy and mortality rate. In terms of molecular characteristics, response to treatment, and clinical appearance, it is also classified as the progesterone receptor (PR), the estrogen receptor (ER), and HER2. The cytochrome P450 aromatase enzyme, which acts as a regulator in estrogen biosynthesis, is involved in the conversion of androstenedione or testosterone into steroidal estrogens. Overexpression of this enzyme has been linked to the formation, progression, and metastasis of ER-positive breast cancers in people who are predisposed to the disease. Furthermore, because estrogen is not produced in postmenopausal women from androgens found in the ovary, it is known that the aromatase enzyme converts androgens into estrogen in organs such as adipose tissue, the brain, blood vessels, skin, bone, and breast tissue. According to a review of the literature, there are not many comprehensive studies aimed at understanding the structure of the aromatase enzyme. The aromatase enzyme has been studied extensively in our current study using bioinformatics tools such as Meta-SNP, Expasy, and HDOCK Server with rational and semi-rational design approaches. Analysis revealed that some amino acid positions in the aromatase enzyme differ significantly from other amino acid positions. Mutations in amino acids at these points may also have an impact on the docking scores as well as affect the physical and chemical properties of this enzyme. Therefore, the results of the current study are believed to bring a different perspective to research on this enzyme.