Studi Molecular Docking Fullerenes C20, C28, C60, C78, C84 dengan Spike Glycoprotein SARS-CoV-2

Abstract

Spike glycoprotein pada SARS-CoV-2 berperan penting dalam proses infeksi virus. Carbon based nanomaterials memiliki banyak alotrop seperti graphene, carbon dots, dan fullerene yang memiliki peran dan interaksi tertentu pada spike glycoprotein. Penelitian ini menggunakan fullerene sebagai ligan dan spike glycoprotein SARS-CoV-2 sebagai reseptor dan mempelajarinya dengan metode molecular docking. Hasil docking didapatkan nilai energi ikat paling negatif dari semua ligan yaitu fullerene C84 dengan nilai -15,9 kcal/mol. Jenis interaksi yang didapatkan yaitu interaksi hidrofobik. Variasi ukuran fullerene mempengaruhi interaksi dan potensi fullerene dalam menginhibisi spike glycoprotein. Berdasarkan targeted docking presentase moda pengikatan sisi aktif reseptor pada fullerene C20 dan C28 sebesar 0%, fullerene C60 sebesar 85%, fullerene C78 dan C84 sebesar 100%. Semakin besar ukuran fullerene maka semakin kuat ikatannya dan potensinya dalam memblok sisi aktif pengikatan ACE2.

The spike glycoprotein in SARS-CoV-2 plays an important role in the viral infection process. Carbon based nanomaterials have many allotropes such as graphene, carbon dots, and fullerenes that have specific roles and interactions in spike glycoproteins. This research used fullerenes as ligands and spike glycoprotein SARS-CoV-2 as receptors and studied them by molecular docking method. The docking results obtained the most negative binding energy value of all ligands, namely fullerene C84 with a value of -15,9 kcal/mol. The type of interaction obtained is a hydrophobic interaction. Variations in the size of fullerenes affected the interaction and potential of fullerenes in inhibiting spike glycoproteins. Based on targeted docking, the percentage of the active site binding mode of the receptor on C20 and C28 fullerenes are 0%, C60 fullerenes are 85%, C78 and C84 fullerenes are 100%. The larger the size of the fullerene, the stronger the bond and its potential to block the active site of ACE2 binding.