Luminescence,
Journal Year:
2024,
Volume and Issue:
39(12)
Published: Dec. 1, 2024
ABSTRACT
In
this
study,
we
employ
spectroscopic,
thermodynamic
and
molecular
docking
approaches
to
identify
the
mechanism
by
which
thiazolidinone
derivatives
4a
–
4d
bind
with
human
serum
albumin.
It
has
been
suggested
that
affinity
of
interaction
HSA
is
within
optimal
range
necessary
for
transportation
distribution
compounds
organism.
The
binding
constant
values
derivative/HSA
complexes
were
found
be
0.03–5.87
×
10
5
M
−1
.
Both
Δ
H
0
S
negative,
indicates
occurs
mainly
through
van
der
Waals
forces
hydrogen
bonding.
negative
calculated
G
indicate
a
spontaneous
process.
Our
study
also
reveals
subdomain
IB
(Site
III)
alters
conformation
stability
HSA.
Molecular
simulations
suggest
main
are
interactions,
hydrophobic
interactions
bonds.
studied
showed
weak
DPPH‐scavenging
activity
at
all
tested
concentrations.
results
compound
4b
phenyl
substituent
nitrogen
atom
1,3‐thiazolidin‐4‐one
moiety
can
considered
most
potent
antioxidant
in
series.
Journal of Molecular Structure,
Journal Year:
2023,
Volume and Issue:
1301, P. 137400 - 137400
Published: Dec. 22, 2023
Two
Schiff
base
ligands
and
some
related
bidentate
tetradentate
Zn(II)
complexes
were
investigated
for
their
biological
activity
profiles
as
anticancer
agents
by
resazurin
method
against
two
leukemia
cell
lines.
The
results
clearly
evidenced
the
importance
of
structure
presence
metal
ion
on
cytotoxicity
profile
these
complexes.
Noteworthy,
they
also
showed
an
interesting
selectivity
index
(SI;
up
to
15.1
complex
[ZnL4(NO3)2]
assessed
PBMC
cells).
electronic
behavior,
stable
geometries,
MEP
surfaces,
FMO
analysis
compounds
employing
density
functional
theory
(DFT)
at
B3LYP
level
with
LANL2DZ/6-311G(d,p)
basic
set.
A
comparison
was
made
computational
experimental
structural
data
L2
[ZnL2(NO3)2]
compounds.
Furthermore,
ensemble
docking
studies
undertaken
a
quadruplex-duplex
(Q-D)
DNA
model
shed
light
interactions
molecular
target.
In
silico
ADME
profiling
performed
using
SwissADME
program,
which
indicated
promising
therapeutic
applicability.
Applied Organometallic Chemistry,
Journal Year:
2024,
Volume and Issue:
39(1)
Published: Oct. 3, 2024
ABSTRACT
Schiff
bases
are
introduced
as
versatile
pharmacophores
for
the
design
and
development
of
various
bioactive
compounds.
Oxime‐based
base
ligands
form
an
important
flexible
class
that
have
attracted
attention
due
to
their
wide
applications
in
fields.
Here,
novel
3‐(2‐hydroxyphenyl‐imino)butan‐2‐one
oxime,
(
HPIO
)
Zn(II)
complexes
derived
from
it,
[Zn(bpy)(HPIO)](NO
3
2
,
C1
(bpy
=
2,2′‐bipyridine)
[Zn(HPIO)
]Cl
C2
were
synthesized
characterized.
Theoretical
studies
showed
both
reactive
high
pharmacological
affinity.
Experimental
investigations
done
compare
some
biological
properties
complexes.
Antioxidant
using
·DPPH
(2,2‐diphenyl‐1‐picrylhydrazyl)
assay
presented
following
trend:
>
.
Considering
importance
antioxidant
enzyme
catalase
removing
oxygen
species
(ROS),
binding
process
/
with
was
evaluated.
Kinetic
can
inhibit
catalytic
performance
by
mixed‐type
inhibition
mechanism.
The
quenched
fluorescence
emission
static
quenching
affinity
higher
than
K
b
1.51
0.89
×
10
5
M
−1
respectively
at
305
K).
In
interaction
catalase,
which
exothermic
spontaneous
process,
hydrogen
bonds,
van
der
Waals
forces,
hydrophobic
interactions
played
a
decisive
role
strongly
confirmed
molecular
docking
data.
Tracking
structural
changes
undergoes
presence
ChemistrySelect,
Journal Year:
2025,
Volume and Issue:
10(7)
Published: Feb. 1, 2025
Abstract
The
study
of
protein‐drug
interactions
has
become
important
in
describing
drug
properties.
Favipiravir
(
Fav
)
is
an
RNA
polymerase
inhibitor
used
to
treat
a
wide
range
influenza
viruses.
This
drug,
which
taken
orally,
can
be
quickly
and
widely
absorbed
the
body.
Here,
interaction
with
two
Fe‐related
proteins,
Catalase
(CAT)
Transferrin
(TF),
was
investigated
by
spectroscopic
molecular
docking
methods.
results
showed
that
strongly
interact
Fe‐proteins
quench
their
intrinsic
fluorescence
through
static
mechanism.
affinity
CAT
TF
almost
close
each
other
order
10
6
M
−1
K
b
=
9.54
×
for
‐TF
10.71
‐CAT
at
310
K).
binding
proteins
changed
conformation
some
extent
stability
decreased.
Molecular
best
site
on
both
along
types
involved.
Hydrogen
bonds
van
der
Waals
were
predominant
forces
observed
between
proteins.
Accessible
surface
area
supports
successful
CAT.
