Artikel Ilmiah : I1C020051 a.n. BETHA VIRGINIA DIAZ PUTRI
| NIM | I1C020051 |
|---|---|
| Namamhs | BETHA VIRGINIA DIAZ PUTRI |
| Judul Artikel | INTERAKSI SENYAWA PHYSALIN TERHADAP INFLAMASOM NLRP3 PADA KANKER SECARA IN SILICO |
| Abstrak (Bhs. Indonesia) | Latar Belakang: Aktivasi inflamasom NLRP3 yang berlebihan dapat menyebabkan perkembangan kanker. Senyawa bahan alam yang tengah dipelajari dapat menghambat aktivasi inflamasom NLRP3 adalah physalin. Penelitian ini bertujuan untuk mengetahui interaksi seluruh tipe physalin terhadap inflamasom NLRP3 pada kanker secara in silico. Metodologi: Molecular docking dilakukan terhadap 20 senyawa uji untuk menentukan nilai energi ikatan serta jenis ikatan. Senyawa terbaik hasil molecular docking dilakukan simulasi molecular dynamics untuk mengetahui interaksi dan kestabilannya pada kondisi fisiologis tubuh. Analisis data dengan membandingkan hasilnya terhadap MCC950. Hasil Penelitian: Tiga senyawa uji dengan nilai energi ikatan terendah yaitu physalin B (-7,2 kkal/mol), physalin M (-7,0 kkal/mol), dan physalin Y (-6,7 kkal/mol). Physalin B dan physalin M membentuk ikatan hidrogen dengan dua residu asam amino kunci Ala228 dan Arg578, sedangkan physalin Y hanya berikatan hidrogen dengan Arg578. Nilai RMSD molecular dynamics physalin B (2,414 Å), physalin M (2,076 Å), dan MCC950 (1,726 Å). Nilai RMSF MCC950 lebih rendah pada residu Ala228 dibandingkan senyawa uji. Namun, pada residu Arg578, physalin M memiliki nilai RMSF lebih rendah dibandingkan MCC950. Energi ikatan physalin B (-59,074,542 kkal/mol), physalin M (-59,791,339 kkal/mol), dan MCC950 (-59,280,897 kkal/mol). Kesimpulan: Physalin M mengikat sisi aktif dan memiliki interaksi yang baik terhadap inflamasom NLRP3. Kata Kunci: kanker, inflamasom NLRP3, physalin, molecular docking, molecular dynamics. |
| Abtrak (Bhs. Inggris) | Background: Excessive activation of the NLRP3 inflammasome can lead to the development of cancer. A natural compound that is being studied to inhibit NLRP3 inflammasome activation is physalin. This study aims to determine the interaction of all types of physalin with the NLRP3 inflammasome in cancer by in silico. Methods: Molecular docking was carried out on 20 test compounds to determine binding energy value and type of bond. The best compound resulting from molecular docking were carried out by molecular dynamics simulations to determine their interactions and stability in the physiological conditions of the body. Data analysis by comparing the results against MCC950. Results: The three test compounds with the lowest bond energy values were physalin B (-7.2 kcal/mol), physalin M (-7.0 kcal/mol), and physalin Y (-6.7 kcal/mol). Physalin B and physalin M form hydrogen bonds with two key amino acid residues Ala228 and Arg578, while physalin Y only hydrogen bonds with Arg578. RMSD molecular dynamics values of physalin B (2.414 Å), physalin M (2.076 Å), and MCC950 (1.726 Å). The RMSF value of MCC950 was lower for residue Ala228 compared to the test compound. However, at residue Arg578, physalin M had a lower RMSF value than MCC950. Binding energy of physalin B (-59,074,542 kcal/mol), physalin M (-59,791,339 kcal/mol), and MCC950 (-59,280,897 kcal/mol). Conclusion: Physalin M binds to the active site and has good interactions with the NLRP3 inflammasome. Keywords: cancer, NLRP3 inflammasome, physalin, molecular docking, molecular dynamics. |
| Kata kunci | kanker, inflamasom NLRP3, physalin, molecular docking, molecular dynamics. |
| Pembimbing 1 | apt. Nur Amalia Choironi, M.Si. |
| Pembimbing 2 | Dr. Muhamad Salman Fareza, M.Si. |
| Pembimbing 3 | |
| Tahun | 2024 |
| Jumlah Halaman | 72 |
| Tgl. Entri | 2024-06-25 11:37:47.727264 |