Analysis Biomolecular Interactions of SARS-CoV-2 Spike Protein and RBD with Immobilized Aptamers by BLI (CAT#: STEM-MB-0098-CJ)

Introduction

Coronaviruses encode four major structural proteins, including spike protein (S), membrane protein (M), envelope protein (E), and nucleocapsid protein (N).SARS-COV-2 S protein is a large protein, ranging in length from 1,160 to 1,400 amino acids. This protein, a coronavirus glycoprotein, contains subunits S1 and S2 that act as trimmers on the virion surface. Spike proteins play a crucial role in the binding of ACE2 receptors to host cells (heart, lungs, etc.) and in the entry of viruses into host cells. RBD has a receptor (RBM) and forms an initial contact with a second ACE2 peptidase, which is a unique Freine (arginine-alanine-arginine-arginine) cleavage at the amino acid site 682-685 of SARS-CoV-2. SARS-COV-2 may regard RBD mutation as an interspecific adaptation during transmission. Mutations in RBD increase the structural stability of spike virus and decrease the binding of vaccine-induced antibodies.