RESUMEN
Effective techniques for the detection of selected viruses detection of their amino acids (AAs) constituents are highly desired, especially in the present COVID pandemic. Motivated by this, we have used density functional theory (DFT) simulations to explore the potential applications of green phosphorene monolayer (GPM) as efficient nanobio-sensor. We have employed van der Waals induced calculations to study the ground-state geometries, binding strength, electronic structures, and charge transfer mechanism of pristine, vacancy-induced and metal-doped GPM to detect the selected AAs, such as glycine, proline and aspartic, in both aqueous and non-aqueous media. We find that the interactions of studied AAs are comparatively weak on pristine (-0.49 to -0.76 eV) and vacancy-induced GPM as compared to the metal-doped GPM (-0.62 to -1.22 eV). Among the considered dopants, Ag-doping enhances the binding of AAs to the GPM stronger than the others. In addition to appropriate binding energies, significant charge transfers coupled with measurable changes in the electronic properties further authenticate the potential of GPM. Boltzmann thermodynamic analysis have been used to study the sensing mechanism under varied conditions of temperatures and pressure for the practical applications. Our findings signify the potential of G PM based sensors towards efficient detection of the selected AAs.
RESUMEN
The prevalence of respiratory illness caused by the novel SARS-CoV-2 virus associated with multiple organ failures is spreading rapidly because of its contagious human-to-human transmission and inadequate globalhealth care systems. Pharmaceutical repurposing, an effective drug development technique using existing drugs, could shorten development time and reduce costs compared to those of de novo drug discovery. We carried out virtual screening of antiviral compounds targeting the spike glycoprotein (S), main protease (Mpro), and the SARS-CoV-2 receptor binding domain (RBD)-angiotensin-converting enzyme 2 (ACE2) complex of SARS-CoV-2. PC786, an antiviral polymerase inhibitor, showed enhanced binding affinity to all the targets. Furthermore, the postfusion conformation of the trimeric S protein RBD with ACE2 revealed conformational changes associated with PC786 drug binding. Exploiting immunoinformatics to identify T cell and B cell epitopes could guide future experimental studies with a higher probability of discovering appropriate vaccine candidates with fewer experiments and higher reliability.