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All Journal Pharmaciana: Jurnal Kefarmasian Indonesian Journal of Cancer Chemoprevention Indonesian Journal of Biotechnology PHARMACY: Jurnal Farmasi Indonesia (Pharmaceutical Journal of Indonesia) JFIOnline Jurnal Farmasi Sains dan Praktis Jurnal Kefarmasian Indonesia
Nunuk Aries Nurulita
Fakultas Farmasi Universitas Muhammadiyah Purwokerto
Biochemistry, Genetics & Molecular Biology Chemistry Health Professions Immunology & microbiology Materials Science & Nanotechnology Medicine & Pharmacology Public Health

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Virtual Screening on Molecules Targeting the Interaction Between Estrogen Receptor Beta and Murine Double Minute 2 Salmasfattah, Novyananda; Nurulita, Nunuk Aries; Dhiani, Binar Asrining
Indonesian Journal of Cancer Chemoprevention Vol 13, No 3 (2022)
Publisher : Indonesian Society for Cancer Chemoprevention

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14499/indonesianjcanchemoprev13iss3pp184-194

Abstract

Estrogen receptor beta (ERβ) is an isoform of estrogen receptor that plays a role in breast cancer. An E3 ubiquitin ligase, murine double minute 2 (MDM2), can bind to ERβ and degrade it. Virtual screening and protein-protein docking studies are one of the approaches that can be performed to discover FDA-approved drugs targeting the interaction of the ERβ-MDM2 complex. This study aimed to conduct virtual screening of 1615 compounds targeting the interaction between ERβ-MDM2 as an initial study to discover potential breast cancer drugs. Biovia Discovery Studio 2021, ClusPro 2.0, PyRx 8.0, and PyMOL software were utilized in this study. ERβ (PDB ID: 3OLS) and MDM2 (PDB ID: 1T4E) receptors were docked to obtain the ERβ-MDM2 protein complex. The ligands used in the virtual screening were FDA-approved drugs downloaded from the ZINC database. PIC and PLIP web tools were also utilized to analyze the amino acid residues involved in the interaction. The virtual screening results showed that ergotamine was the drug with the lowest energy score (-12.0 kcal/mol) among 1057 drugs and was able to establish the strongest interaction between ERβ-MDM2. In conclusion, based on this computational study, ergotamine strengthens the interaction between ERβ-MDM2 and thus could be used as a candidate for breast cancer drug. Thorough validation of in vitro, biochemical, and in vivo studies are needed to confirm this finding.Keywords: Estrogen receptor beta, breast cancer, protein-protein interaction, MDM2.
Protein-protein Docking Studies of Estrogen Receptor Alpha and TRIM56 Interaction for Breast Cancer Drug Screening Dhiani, Binar Asrining; Nurulita, Nunuk Aries; Fitriyani, Fitriyani
Indonesian Journal of Cancer Chemoprevention Vol 13, No 1 (2022)
Publisher : Indonesian Society for Cancer Chemoprevention

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14499/indonesianjcanchemoprev13iss1pp46-54

Abstract

Breast cancer is the highest mortality cause in women with cancer. Protein-protein docking for target-based screening is an effective approach in breast cancer drug discovery via estrogen receptor (ER) signaling. TRIM56, an E3 ubiquitin protein ligase, can bind to and stabilize ER alpha. Thus, drug screening that can inhibit or weaken the interaction between ER alpha and TRIM56 is promising to obtain novel yet specific breast cancer drugs. In this study, we performed protein-protein docking studies for ER alpha and TRIM56 interaction and virtual screening for FDA-approved drugs from the ZINC database against ER alpha and TRIM56 complex protein model structure. We utilized Cluspro 2.0, PyRx 0.8, and Pymol 2.4.1 to conduct protein-protein docking, virtual screening, and model structure visualization. PIP and PLIP software were also applied to analyze the amino acid residue between proteins or protein-ligands. Based on the protein-protein docking, ER alpha and TRIM56 established interaction. Utilizing this complex protein as a macromolecule in the virtual screen of 1071 molecules of FDA-approved drugs, we obtain the top five lowest binding energy molecules i.e., dutasteride, dihydroergotamine, nilotinib, ergotamine, and bromocriptine. In addition, the energy binding affinity between ER alpha-dutasteride complex with TRIM56 was weakened in the presence of dutasteride. In conclusion, protein-protein docking between ER alpha-TRIM56 was able to select FDA-approved drugs that could bind to the complex, and dutasteride binding to ER alpha-TRIM56 complex weakened the interaction.Keywords: protein-protein docking, estrogen receptor alpha, TRIM56, breast cancer, ubiquitin.
Co-Authors . Sugiyanto Agus Siswanto Anjar Mahardian Kusuma Arif Wirahadi Kusuma, Arif Wirahadi Binar Asrining Dhiani Cindy Caesaria, Cindy Darsini Darsini Della Caya Nur Syarifah Dwi Hartanti Edy Meiyanto Edy Meiyanto Edy Meiyanto Eishou Matsuda Elza Sundhani Fitriyani Fitriyani Ika Puspitasari Imam Purnomo Sugiarto, Imam Purnomo Lita Ratriyana Zumrohani Masashi Kawaichi Nastiti, Nindita Sari Salmasfattah, Novyananda Septiadi, Binaripan Sharas Swara Maulita, Sharas Swara Solehah, Senja Nur Sugiyanto Sugiyanto Sundhani, Elza Susanti Susanti Tjiptasurasa Tjiptasurasa, Tjiptasurasa Veby Tri Yulianti Weny Delvia Yuniarti, Azizah