<![CDATA[In the last decade, cancer treatment get into a new era called targeted therapy for cancer. Monoclonal antibody (mAb) is one of the targeted therapy agents and belongs to a part of passive immunotherapy. The aim of this study is to predict the relative strength of binding affinity for several monoclonal antibodies binding to HER-1 and HER-2 receptors by calculating dissociation constants, evaluating a dominant interaction of the complexes, and predict the reactivity of HER-1 and HER-2 according to potential electrostatic map. Structures of the complexes of mAB (cetuximab and nimotuzumab) with HER-1 and anti-HER-2 (trastuzumab and petuzumab) with HER-2 was generated by docking simulation which combine three docking protocols (ZDOCK, ZRANK, and RDOCK). Filtering the initial docked poses with CDR’s (Complementarity Determining Regions) residues of antibody and the binding site of residues was done to narrow the resulted poses. The result of this study show that generally, the interaction between chimeric and humanized monoclonal antibodies with HER-1 present polar-polar interaction from lysine, asparagin, serin, arginin, and glutamin amino acids, and both of mAb interacted with domain III of HER-1, whereas, interaction between humanized monoclonal antibodies with HER‑2 was dominated by polar-polar interaction from aspartic acid, glutamic acid, glutamin, and lysin amino acids with domain II and IV of HER-2.*****Pada dekade terakhir, pengobatan kanker memasuki era baru yang disebut terapi kanker terarah. Antibodi monoklonal (mAb) adalah salah satu jenis obat terapi terarah yang merupakan bentuk pasif dari imunoterapi. Tujuan dari penelitian ini adalah memprediksi kekuatan relatif afinitas pengikatan kompleks-kompleks yang terbentuk dari hasil simulasi doking dengan menghitung tetapan disosiasinya, menginventarisasi jenis-jenis interaksi yang dominan, dan memprediksi reaktifitas HER-1 dan HER-2 berdasarkan pemetaan potensial elektrostatik molekul. Struktur kompleks tiga dimensi kompleks antibodi monoklonal anti-HER-1 (cetuximab dan nimotuzumab) dengan reseptor HER-1 dan antibodi monoklonal anti-HER‑2 (trastuzumab dan pertuzumab) dengan reseptor HER-2 ditentukan menggunakan metode doking protein-protein yang mengkombinasikan antara protokol pencarian ZDOCK dan fungsi skor ZRANK, serta protokol perbaikan pose RDOCK. Penyaringan hasil pose dilakukan berdasarkan sekuen asam-amino di daerah CDR (Complementarity Determining regions) dari antibodi dan sisi binding dari reseptor. Hasil penelitian yang diperoleh menunjukkan bahwa secara umum interaksi antara antibodi monoklonal chimeric dan humanized dengan HER-1 digambarkan oleh interaksi polar-polar dari asam-asam amino lisin, asparagin, serin, arginin, dan glutamin serta keduanya berinteraksi di domain III HER-1, edangkan interaksi antara antibodi monoklonal humanized dengan HER‑2 didominasi oleh interaksi polar-polar dari asam-asam amino aspartat, glutamat, glutamin, dan lisin di domain II dan IV HER-2.]]>
