Dual inhibition of S. aureus TyrRS and S. aureus gyrase by two 4-amino-4 ′ -acetyldiphenyl sulfide-based Schiff bases: Structural features, DFT study, Hirshfeld surface analysis and molecular docking
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Date
2022-07-19
Authors
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Abstract
Two 4-amino-4
′
-acetyldiphenyl sulfide-based Schiff bases, namely 1-[4-({4-[(E)-(2-hydroxynaphthalen-1-yl)
methylideneamino]phenyl}sulfanyl)-phenyl]ethanone (I) and (E)-1-[4-({4-[(4-methoxybenzylidene)amino]
phenyl}-sulfanyl)phenyl]ethan-1-one (II) were structurally studied. They crystallize respectively in the monoclinic
Cc and the triclinic P1 space groups, with the respective cell parameters: [10.695(3) Å, 44.458(14) Å,
4.4437(11) Å, 99.004(9)
◦
] and [5.7708(2) Å, 8.0867(3) Å, 19.6929(8) Å, 81.844(2)
◦
, 86.664(3)
].
The asymmetric units of (I) and (II) are composed of one molecule and two crystallographically independent
molecules, respectively. Their molecular structures were optimized by the density functional theory and correlated
correspondingly
to
the
crystal
structures.
Moreover,
the
IR
vibration
modes
were
assigned
to
the
calculated
wavenumbers,
the
Mulliken
atomic
charges
obtained
and
the
frontier
molecular
orbitals
evaluated.
The
hydrogen
bonding
and the non-classical intermolecular interactions within the two frameworks were investigated using
Hirshfeld surface analysis which indicated the presence of C
–
H…H
–
C, C
–
H⋅⋅⋅π, C
–
H⋅⋅⋅O, C
and
π⋅⋅⋅lp interactions as well as π⋅⋅⋅π stacking. Additionally, in order to understand the interacting binding sites
of the two molecules with the bacterial S. aureus protein receptors, the studied compounds were in silico evaluated
by molecular docking against tyrosyl-tRNA synthetase 1JIJ and topoisomerase II DNA gyrase 2XCT enzymes.
The results revealed consequently potent antimicrobial efficacy through the formed hydrogen bonds,
hydrophobic contacts,
π-cation interactions and π…π stacking.
◦
, 85.662(3)
–
H⋅⋅⋅N, C
◦
–
H⋅⋅⋅S