<![CDATA[ABSTRAKPenggunaan tumbuhan masih menjadi pilihan utama penduduk Indonesia sebagai pengobatan alternatif. Tumbuhan jeringau (Acorus calamus L) adalah salah satu tumbuhan dengan beberapa senyawa penting telah dilaporkan aktif sebagai antidiabetes melalui mekanisme peningkatan produksi dan fungsi insulin, juga melalui mekanisme inhibisi fungsi enzim α-glucosidase. Peneliti berupaya melanjutkan penelusuran antidiabetes melalui mekanisme inhibisi enzim α-glucosidase manusia menggunakan metode in silico. Ligan uji dan kontrol ditelusuri dari kepustakaan dan diunduh berdasarkan data canonical “SMILES”, selanjutnya dikonversi ke struktur 3D. Reseptor α-glucosidase manusia dimodelkan melalui teknik “Molecular Homology” berdasarkan sequence α-glucosidase manusia yang diunduh dari GenBank dengan kode ABI53718.1. Sedangkan template reseptor α-glucosidase manusia tersebut diunduh dari Protein Data Bank (Pdb id. 3W37). Metode in silico yang digunakan meliputi teknik “Homology Molecular dan Docking Molecuar”. Hasil pemodelan α-glucosidase manusia menunjukkan 88.59% struktur model masuk dalam core region Ramachandran Map dengan 17 residu asam amino pada dissalowed region, namun masih dalam batas persyaratan model berkualitas baik. Hasil docking menunjukkan kemampuan 7 ligan uji berinteraksi dengan reseptor α-glucosidase manusia lebih lemah dibanding ligan kontrol acarbose, namun semua ligan uji masih menunjukkan pelepasan energi dengan nilai afinitas terendah -9.98 kcal/mol dan tertinggi -12.61 kcal/mol masing-masing oleh humulen dan acoradine. Hasil visualisasi interaksi semua ligan uji (α-asaron, β-asaron, acoranon, acoramon, acoradin, eugenol, dan humulen juga menunjukkan pola interaksi yang mirip dengan ligan kontrol pada daerah binding site yang sama, sehingga semua ligan uji berpotensi sebagai inhibitor α-glucosidase manusia.ABSTRACTThe use of plants is still the main choice for Indonesians as alternative medicine. Jeringau plant (Acorus calamus L) is one of the plants with several important compounds that have been reported to be active as antidiabetics through the mechanism of increasing insulin production and function, as well as through the mechanism of inhibition of the function of the -glucosidase enzyme. Researchers are trying to continue the search for antidiabetic through the mechanism of inhibition of the human α-glucosidase enzyme through the in silico method. The test and control ligands were traced from the literature and downloaded based on the “SMILES” canonical data, then converted to a 3D structure. The human α-glucosidase receptor was modeled using the “Molecular Homology” technique based on the human α-glucosidase sequence downloaded from GenBank with code ABI53718.1. The human α-glucosidase receptor template was downloaded from the Protein Data Bank (Pdb id. 3W37). The in silico method used includes the "Molecular Homology and Molecular Docking" technique. The results of human α-glucosidase modeling showed that 88.59% of the model structure was included in the core region of the Ramachandran Map with 17 amino acid residues in the dissalowed region, but it was still within the limits of good quality model requirements. The docking results showed the ability of the 7 test ligands to interact with the human -glucosidase receptor was weaker than the acarbose control ligand, but all test ligands still showed energy release with the lowest affinity value of -9.98 kcal/mol and the highest -12.61 kcal/mol respectively by humulen and acoradine. The results of visualization of the interaction of all the test ligands (α-asaron, β-asaron, acoranon, acoramon, acoradin, eugenol, dan humulen) also showed an interaction pattern similar to the control ligand at the same binding site area, so that all the tested ligands were potential as human α-glucosidase inhibitors.]]>
