Identification Of Natural Compounds and Selective Inhibitors Targeting Ptps, PTP1B And ABCG2 Using Molecular Docking and Screening Tools Against Breast Cancer.
The prevalence of breast cancer continues to rise, making them one of the most common diseases worldwide. In response, we have focused on inhibiting key proteins associated with this disease, specifically PTPs, PTP1B, and ABCG2. Our study began by examining over 23 indigenous plants from Chlef, Algeria, ultimately selecting fenugreek, date seeds, and mandarin peel for further analysis. A pharmacoinformatics study was conducted on 11 molecules from a pool of 75, demonstrating the potential inhibitory effects of rutin, Lutein, and naringin. Specifically, rutin showed an inhibitory interaction with PTPs, forming 1 amino acid bonds with a binding energy of ∆G = -5.3358 kcal/mol, while Naringin interacted with PTP1B, forming 3 amino acid bonds with a binding energy of ∆G = -7.2124 kcal/mol. Lutein formed 0 bonds with ABCG2, with a binding energy of ∆G = -6.5143 kcal/mol. The binding energy analysis of Tamoxifen across different protein targets shows varying degrees of interaction. The highest binding affinity is observed with 6VXI (-5.51 kcal/mol), followed by IXBO (-5.19 kcal/mol), while the weakest interaction occurs with 3I2B (-4.93 kcal/mol).