tetano
Editor, Senior Moderator
J Biomol Struct Dyn
. 2021 Dec 14;1-18.
doi: 10.1080/07391102.2021.2014973. Online ahead of print.
Elucidating the role of N440K mutation in SARS-CoV-2 spike - ACE-2 binding affinity and COVID-19 severity by virtual screening, molecular docking and dynamics approach
Malathi Kullappan[SUP] 1 [/SUP], Usha Mary[SUP] 2 [/SUP], Jenifer M Ambrose[SUP] 1 [/SUP], Vishnu Priya Veeraraghavan[SUP] 3 [/SUP], Krishna Mohan Surapaneni[SUP] 1 4 5 6 [/SUP]
Affiliations
Abstract
COVID-19 has become a public health concern around the world. The frequency of N440K variant was higher during the second wave in South India. The mutation was observed in the Receptor Binding Domain region (RBD) of the Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2) spike (S) protein. The binding affinity of SARS-CoV-2-Angiotensin-Converting Enzyme-2 (ACE-2) plays a major role in the transmission and severity of the disease. To understand the binding affinity of the wild and mutant SARS-CoV-2 S with ACE2, molecular modeling studies were carried out. We discovered that the wild SARS-CoV-2 S RBD-ACE-2 complex has a high binding affinity and stability than that of the mutant. The N440K strain escapes from antibody neutralization, which might increase reinfection and decrease vaccine efficiency. To find a potential inhibitor against mutant N440K SARS-CoV-2, a virtual screening process was carried out and found ZINC169293961, ZINC409421825 and ZINC22060839 as the best binding energy compounds. Communicated by Ramaswamy H. Sarma.
Keywords: COVID-19; SARS-CoV-2; binding energy; elbasvir analogues; maraviroc analogues; public health; simeprevir analogues.
. 2021 Dec 14;1-18.
doi: 10.1080/07391102.2021.2014973. Online ahead of print.
Elucidating the role of N440K mutation in SARS-CoV-2 spike - ACE-2 binding affinity and COVID-19 severity by virtual screening, molecular docking and dynamics approach
Malathi Kullappan[SUP] 1 [/SUP], Usha Mary[SUP] 2 [/SUP], Jenifer M Ambrose[SUP] 1 [/SUP], Vishnu Priya Veeraraghavan[SUP] 3 [/SUP], Krishna Mohan Surapaneni[SUP] 1 4 5 6 [/SUP]
Affiliations
- PMID: 34904526
- DOI: 10.1080/07391102.2021.2014973
Abstract
COVID-19 has become a public health concern around the world. The frequency of N440K variant was higher during the second wave in South India. The mutation was observed in the Receptor Binding Domain region (RBD) of the Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2) spike (S) protein. The binding affinity of SARS-CoV-2-Angiotensin-Converting Enzyme-2 (ACE-2) plays a major role in the transmission and severity of the disease. To understand the binding affinity of the wild and mutant SARS-CoV-2 S with ACE2, molecular modeling studies were carried out. We discovered that the wild SARS-CoV-2 S RBD-ACE-2 complex has a high binding affinity and stability than that of the mutant. The N440K strain escapes from antibody neutralization, which might increase reinfection and decrease vaccine efficiency. To find a potential inhibitor against mutant N440K SARS-CoV-2, a virtual screening process was carried out and found ZINC169293961, ZINC409421825 and ZINC22060839 as the best binding energy compounds. Communicated by Ramaswamy H. Sarma.
Keywords: COVID-19; SARS-CoV-2; binding energy; elbasvir analogues; maraviroc analogues; public health; simeprevir analogues.