Computational modeling of the effect of five mutations on the structure of the ACE2 receptor and their correlation with infectivity and virulence of some emerged variants of SARS-CoV-2 suggests mechanisms of binding affinity dysregulation

Ultrasound-assisted extraction of emodin from Rheum officinale Baill and its antibacterial mechanism against Streptococcus suis based on CcpA

“…Similarly, the mutation of TYR130, GLY189 and GLY197 affected the affinity of CcpA with emodin. In common, the decrease in affinity was due to the lack of interaction between some of the key residues [78] . In this study, the main affinity between emodin and CcpA came from hydrogen bonding, which was located outside the mutation region that could not be speculated by 3D modeling [55] .…”

“…In this study, the main affinity between emodin and CcpA came from hydrogen bonding, which was located outside the mutation region that could not be speculated by 3D modeling [55] . Therefore, the increase and decrease in the affinity between emodin and CcpA were probably related to the formation or loss of new interactions between the mutation of amino acids residues [78] .…”

Combining MOE Bioinformatics Analysis and In Vitro Pseudovirus Neutralization Assays to Predict the Neutralizing Ability of CV30 Monoclonal Antibody on SARS-CoV-2 Variants

“…Numerous scholars have proposed various methods to forecast the changes in binding free energy (BFE) resulting from mutations, including the TopNetTree model [ 5 ], MutaBind2 method [ 6 ], SAAMBE-SEQ method [ 7 ], SAAMBE-3D method [ 8 ], and so on. A study [ 9 ] used a bioinformatics molecular docking approach to predict the impact of the angiotensin-converting enzyme 2 (ACE2) receptor when interacting with the receptor binding domain (RBD) of five new coronavirus variants (Alpha, Beta, Gamma, Delta, and Omicron). The results showed that these variants can alter the interaction of S and human ACE2 proteins, lose or create new interprotein contacts, enhance viral fitness by increasing binding affinity, and increase infectivity, virulence, and transmissibility.…”