Single-Molecule Investigation of the Binding Interface Stability of SARS-CoV-2 Variants with ACE2

The novel coronavirus SARS-CoV-2 has caused a global pandemic, and much research is being done to understand the virus and find ways to combat it. Oneimportant aspect of this research is the study of the binding interface between the virus and human receptors. This interface plays a crucial role in virustransmission and is a potential target for therapeutic intervention. In this study, the binding interface between the receptor-binding domain (RBD) ofSARS-CoV-2 and the ACE2 receptors was investigated using atomic force microscopy and steered molecular dynamics. The aim was to understand theimpact of variants of concern on the binding affinity between RBD and ACE2. Results showed that some of the latest variants have a stronger bindingaffinity, leading to the possibility of immune escape. The findings of this study provide important insights into the dynamics of the RBD-ACE2 interaction andcan inform the development of new strategies for combating SARS-CoV-2. This research highlights the importance of continued monitoring and study of thevirus and its variants to effectively control its spread and minimize its impact on public health.