ANALISIS MUTASI GEN rpoB PADA Mycobacterium tuberculosis RESISTEN RIFAMPISIN DI INDONESIA MENGGUNAKAN METODE BIOINFORMATIKA

YUNITA ANGGRAENI, - (2025) ANALISIS MUTASI GEN rpoB PADA Mycobacterium tuberculosis RESISTEN RIFAMPISIN DI INDONESIA MENGGUNAKAN METODE BIOINFORMATIKA. Skripsi thesis, Sekolah Tinggi Farmasi Indonesia.

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Abstract

Tuberkulosis masih menjadi tantangan kesehatan global, dengan Indonesia termasuk negara dengan salah satu kasus resistensi obat tertinggi. Rifampisin sebagai obat lini pertama bekerja dengan menghambat enzim RNA polymerase subunit β (rpoB), namun mutasi pada gen ini dapat menurunkan efektivitasnya. Penelitian ini bertujuan menganalisis pengaruh mutasi D435V (mutan 1), H445Y (mutan 2), dan S450L (mutan 3) pada gen rpoB terhadap interaksi rifampisin serta membandingkan afinitas pengikatannya menggunakan metode penambatan molekul. Struktur protein native (PDB ID: 5UAC) dan model mutan diperoleh melalui Swiss-Model, sedangkan penambatan dilakukan menggunakan AutoDock4 dan divisualisasikan dengan BIOVIA Discovery Studio. Hasil menunjukkan bahwa energi pengikatan rifampisin terhadap protein native sebesar -6,64 kkal/mol, sedangkan pada mutan 1, 2, dan 3 masing-masing -6,30, -6,60, dan -6,73 kkal/mol. Mutan 2 dan 3 menyebabkan perubahan interaksi yang signifikan dengan hilangnya beberapa ikatan hidrogen penting, sehingga menurunkan kestabilan kompleks ligan–reseptor. Dengan demikian, mutasi pada gen rpoB berpengaruh terhadap afinitas dan stabilitas pengikatan rifampisin, yang menjadi dasar molekuler resistensi rifampisin pada Mycobacterium tuberculosis. ----- Tuberculosis remains a global health challenge, including Indonesia, a country with one of the highest drug resistance cases. Rifampicin as a first-line drug works by inhibiting the RNA polymerase subunit β (rpoB) enzyme, but mutations in this gene can reduce its effectiveness. This study aims to analyze the effect of mutations D435V (mutant 1), H445Y (mutant 2), and S450L (mutant 3) in the rpoB gene on rifampicin interactions and compare their binding affinities using molecular docking methods. The native protein structure (PDB ID: 5UAC) and mutant models were obtained through Swiss-Model, while docking was performed using AutoDock4 and visualized with BIOVIA Discovery Studio. The results showed that the binding energy of rifampicin to the native protein was -6.64 kcal/mol, while in mutants 1, 2, and 3 it was -6.30, -6.60, and -6.73 kcal/mol, respectively. Mutants 2 and 3 cause significant interaction changes with the loss of several key hydrogen bonds, thus decreasing the stability of the ligand-receptor complex. Thus, treatment of the rpoB gene affects the affinity and stability of rifampin, which is the molecular basis of rifampin resistance in Mycobacterium tuberculosis.

Item Type:	Thesis (Skripsi)
Uncontrolled Keywords:	Mycobacterium tuberculosis, rpoB, rifampisin, penambatan molekul, resistensi obat. ---- Mycobacterium tuberculosis, rpoB, rifampin, molecular docking, drug resistance
Subjects:	Q Science > Q Science (General) Q Science > QA Mathematics > QA75 Electronic computers. Computer science
Divisions:	Program Studi S1 Farmasi
Depositing User:	pustakawan - -
Date Deposited:	17 Nov 2025 06:52
Last Modified:	17 Nov 2025 06:52
URI:	http://repository.stfi.ac.id/id/eprint/3463

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