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All Journal Jurnal Pendidikan Biologi Undiksha Wahana-Bio: Jurnal Biologi dan Pembelajarannya Jurnal Pembelajaran dan Biologi Nukleus Jurnal Ilmiah Biologi Eksperimen dan Keanekaragaman Hayati (J-BEKH) Konservasi Hayati BERNAS: Jurnal Pengabdian Kepada Masyarakat Lumbung Inovasi: Jurnal Pengabdian Kepada Masyarakat Indonesian Journal of Medical Chemistry and Bioinformatics Maximus: Journal of Biological and Life Sciences Jurnal Bioteknologi & Biosains Indonesia (JBBI) Indonesian Journal of Jamu Jurnal Bioteknologi & Biosains Indonesia
Khaerunissa Anbar Istiadi
Program Studi Biologi, Institut Teknologi Sumatera, Lampung Selatan, Lampung, Indonesia 35365
Religion Agriculture, Biological Sciences & Forestry Humanities Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Computer Science & IT Dentistry Education Environmental Science Health Professions Immunology & microbiology Languange, Linguistic, Communication & Media Mathematics Medicine & Pharmacology Neuroscience Nursing Public Health Social Sciences Veterinary Other

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Journal : Indonesian Journal of Medical Chemistry and Bioinformatics

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A Computational Exploration: Docking Analysis of Compounds from Foeniculum vulgare as Potential Aromatase Inhibitors for Endometriosis Candidate Therapy Suryandari, Dwi Anita; Sari, Puji; Sunaryo, Hadi; Istiadi, Khaerunissa Anbar
Indonesian Journal of Medical Chemistry and Bioinformatics Vol. 2, No. 2
Publisher : UI Scholars Hub

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Aromatase inhibitors (AI) have controlling symptoms and size of endometriotic implants, making them a promising second-line therapy for endometriosis treatment.pretreatment with letrozole, an AI, combined with leuprolide acetate and resveratrol has been found to improve in vitro fertilization (IVF) outcomes in women mild endometriosis.in this study we screening and analysis of ten phenolic compounds from Foeniculum vulgare using molecular docking with Mcole server.from this results showed that three phenolic trans resveratrol (TR), caempherol coumaril (CC) have low gibbs energy compare with resveratrol (R). The binding modalities of compound TR and compound R were hydrogen-bonding between the hydroxyl and oxygen atom and Thr310 and hydrophobic interactions with Phe187, Ala272, Asp275, Ala189.and compound R exhibited cation-π interactions between Val336 as binding activity from aromatase.aromatase inhibitors and resveratrolfrom fennel lies in the potential of resveratrol to modulate hormonal pathways, including aromatase inhibition.
Molecular Insights into Propylthiouracil as a Thyroid Peroxidase Inhibitor: A Computational Study Approach Suryandari, Dwi Anita; Yunaini, Luluk; Sunaryo, Hadi; Istiadi, Khaerunissa Anbar; Pratomo, Irandi Putra
Indonesian Journal of Medical Chemistry and Bioinformatics Vol. 3, No. 1
Publisher : UI Scholars Hub

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Thyroid peroxidase (TPO) is a crucial enzyme in the biosynthesis of thyroid hormones, catalyzing the iodination of tyrosine residues in thyroglobulin and the coupling of iodotyrosines to form thyroxine (T4) and triiodothyronine (T3). Propylthiouracil (PTU) is an antithyroid drug commonly used to manage hyperthyroidism by inhibiting TPO. Understanding the molecular interactions between TPO and PTU can provide insights into the inhibitory mechanisms and guide the design of more effective antithyroid medications. Objective: This study aims to elucidate the binding interactions between TPO and PTU through molecular docking, providing a detailed understanding of how PTU inhibits TPO activity. Methods: The three-dimensional structure of TPO was obtained from Prosite and modelling by swissmodel and prepared for docking. The structure of PTU was optimized, and molecular docking was performed using AutoDock. The binding affinity, binding poses, and key interactions between TPO and PTU were analyzed. Visualization of the docking results was performed using PyMOL to identify critical residues involved in PTU binding. Results: The docking analysis revealed that PTU binds effectively to the active site of TPO with a binding affinity of -5.45 kcal/mol. The interaction involves coordination with the heme group and several key residues, including His239, which coordinates the heme, and Ser314, which forms hydrogen bonds with PTU. Additionally, hydrophobic interactions with residues Phe241 and Ile399 stabilize the binding of PTU in the active site. Conclusion: The docking study highlights the significant interactions between PTU and TPO, elucidating the molecular basis of TPO inhibition by PTU. The binding affinity and key interactions identified in this study provide a foundation for the design of more potent antithyroid drugs.
Co-Authors Aji Hafidz Talaga Alawiyah, Alawiyah Alfauzia, Nadia Amelia, Tiara Andreas Dwi Nugroho Andriani, Silvia Aniesti, Frigia Rafilia Anisa, Hida Arliani Nur Ariyanto, Dika Ariyanto Astuti, Ayu Widia Desi Budiono Deviany Deviany, Deviany Dewi Chusniasih DINA ANGGRAINI Dini Meilinda Dwi Anita Suryandari Erma Suryanti Fajri Arif Wibawa Fatimatuzzahra, Izza Fatriani, Rizka Febrina, Yane Fita Feerzet Achmad Ferdinanda, Thierry Garbono, Andrian Gres Maretta, Gres Hadi Sunaryo Handayani, Catie Hariyandi, Yopi Hida Arliani Nur Anisa Iffa Afiqa Khairani Imaniar, Lisana Husna Irandi Putra Pratomo Jannah, Umi Nur Luluk Yunaini Muhyi, Abdul Mulyana, Jeane Siswitasari Nur Anisa, Hida Arliani Puji Sari Reni Yuniarti Restiawati, Nawang Sari, Dian Anggria Satria, Arysca Wisnu Siragih, Rajuman S Suryanti, Erma Triya Yuli Andini Yuni Sukmawati Yusuf, Reggina Aulia Zhofiroh, Nawrah Meisyah Muthi'ah