In the title compound, C(16)H(16)N(2)OS, the conformation at the two partially double C-N bonds of the thio-urea unit is E. The amide group is twisted relative to the thio-urea fragment, forming a dihedral angle of 62.44 (16)°, and the two phenyl rings form a dihedral angle 75.93 (18)°. In the crystal, mol-ecules are linked by N-H⋯S hydrogen bonds, forming centrosymmetric dimers.
In the title compound, C(14)H(12)N(2)O(2)S, the amino-phenol and the benzoyl groups adopt a syn-anti configuration with respect to the thiono C=S group across the thio-urea C-N. The dihedral angle between the mean planes of the benzoyl and hy-droxy-phenyl rings is 36.77 (8)°. The mol-ecules are stabilized by intra-molecular N-H⋯O hydrogen bonds. In the crystal, weak inter-molecular C-H⋯O, O-H⋯S and N-H⋯O hydrogen bonds link the mol-ecules into a chain along the c axis.
In the title compound, C(13)H(16)N(2)OS, the piperidine ring exhibit a classical chair conformation. In the crystal, the mol-ecules are linked by N-H⋯O hydrogen bonds, forming zigzag chains running parallel to the c axis.
Over the course of the COVID-19 pandemic, several SARS-CoV-2 variants have emerged that may exhibit different etiological effects such as enhanced transmissibility and infectivity. However, genetic variations that reduce virulence and deteriorate viral fitness have not yet been thoroughly investigated. The present study sought to evaluate the effects of viral genetic makeup on COVID-19 epidemiology in Pakistan, where the infectivity and mortality rate was comparatively lower than other countries during the first pandemic wave. For this purpose, we focused on the comparative analyses of 7096 amino-acid long polyprotein pp1ab. Comparative sequence analysis of 203 SARS-CoV-2 genomes, sampled from Pakistan during the first wave of the pandemic revealed 179 amino acid substitutions in pp1ab. Within this set, 38 substitutions were identified within the Nsp3 region of the pp1ab polyprotein. Structural and biophysical analysis of proteins revealed that amino acid variations within Nsp3's macrodomains induced conformational changes and modified protein-ligand interactions, consequently diminishing the virulence and fitness of SARS-CoV-2. Additionally, the epistatic effects resulting from evolutionary substitutions in SARS-CoV-2 proteins may have unnoticed implications for reducing disease burden. In light of these findings, further characterization of such deleterious SARS-CoV-2 mutations will not only aid in identifying potential therapeutic targets but will also provide a roadmap for maintaining vigilance against the genetic variability of diverse SARS-CoV-2 strains circulating globally. Furthermore, these insights empower us to more effectively manage and respond to potential viral-based pandemic outbreaks of a similar nature in the future.