<![CDATA[Abstrak Resistensi antibiotik terhadap Staphylococcus aureus, khususnya strain Methicillin-Resistant Staphylococcus aureus (MRSA), merupakan tantangan besar dalam pengobatan infeksi bakteri. Salah satu protein virulensi penting dari S. aureus adalah Clumping factor B (ClfB), yang berperan dalam proses adhesi dan pembentukan biofilm pada jaringan inang. Penghambatan protein ini dapat menurunkan kemampuan kolonisasi bakteri, sehingga menjadi target potensial dalam pengembangan agen antibakteri baru. Penelitian ini bertujuan untuk mengevaluasi potensi kuersetin dari daun binahong (Anredera cordifolia) sebagai inhibitor alami terhadap protein ClfB secara in silico. Struktur tiga dimensi protein ClfB diperoleh dari Protein Data Bank (PDB), sedangkan struktur kuersetin diunduh dari basis data PubChem. Proses molecular docking dilakukan menggunakan SwissDock dengan analisis lanjutan melalui UCSF Chimera. Hasil docking menunjukkan bahwa kuersetin berikatan kuat pada kantong aktif ClfB dengan nilai afinitas energi sebesar −7,584 kcal/mol, menandakan kestabilan kompleks yang baik secara termodinamika. Interaksi yang terbentuk melibatkan residu asam amino polar seperti Ser, Glu, dan Asp serta residu nonpolar seperti Leu dan Val yang berkontribusi terhadap pengikatan stabil. Visualisasi struktur menunjukkan bahwa kuersetin menempati sisi aktif ClfB dan berpotensi menghambat fungsi adhesi protein tersebut. Berdasarkan hasil ini, kuersetin dari daun binahong berpotensi menjadi kandidat inhibitor alami ClfB yang dapat mengganggu proses kolonisasi S. aureus pada jaringan inang. Penelitian ini memberikan dasar ilmiah bagi pengembangan agen antibakteri berbasis bahan alam dalam upaya mengatasi resistensi antibiotik. Kata kunci: Staphylococcus aureus; ClfB; kuersetin; binahong; antibakteri. Abstrack Antibiotic resistance in Staphylococcus aureus, particularly Methicillin-Resistant Staphylococcus aureus (MRSA), poses a serious challenge to the treatment of bacterial infections worldwide. Clumping factor B (ClfB) is an important virulence protein of S. aureus that plays a crucial role in bacterial adhesion and biofilm formation on host tissues. Inhibition of this protein may reduce bacterial colonization and represents a promising target for novel antibacterial strategies. This study aimed to evaluate the potential of quercetin, an active compound derived from binahong leaves (Anredera cordifolia), as a natural inhibitor of the ClfB protein using an in silico approach. The three-dimensional structure of ClfB was obtained from the Protein Data Bank, while the molecular structure of quercetin was retrieved from the PubChem database. Molecular docking was performed using SwissDock, and the interaction analysis and visualization were conducted using UCSF Chimera. The docking results showed that quercetin exhibited a strong binding affinity toward the active site of ClfB, with a binding energy of −7.584 kcal/mol, indicating favorable thermodynamic stability of the ligand–protein complex. Several polar amino acid residues, including serine, glutamate, and aspartate, as well as nonpolar residues such as leucine and valine, were involved in stabilizing the interaction. Structural visualization confirmed that quercetin occupies the active pocket of ClfB, suggesting its ability to interfere with bacterial adhesion mechanisms. Overall, quercetin from binahong leaves demonstrates potential as a natural ClfB inhibitor and provides a scientific basis for the development of alternative antibacterial agents to address antibiotic resistance in Staphylococcus aureus and support future antimicrobial research. Keywords: Staphylococcus aureus; ClfB; quercetin; binahong; antibacterial.]]>
