In
this
study,
a
comprehensive
investigation
was
undertaken
to
elucidate
simple
triazole
compound,
5-phenyl-1-(p-tolyl)-1H-1,2,3-triazole
(PPTT),
its
interactions
with
high-abundant
proteins
and
identification
of
low-abundant
by
serum
proteomics.
Employing
combination
spectroscopic
techniques
computational
chemistry,
the
between
PPTT
three
high-abundance
blood
globular
proteins,
namely
human
albumin
(HSA),
immunoglobulin
G
(HIgG),
hemoglobin
(BHb),
were
explored,
thereby
ascertaining
their
binding
constants
thermodynamic
parameters
at
molecular
level.
Subsequently,
based
on
differential
proteomics,
utilizing
two-dimensional
gel
electrophoresis
(2-DE)
in
conjunction
matrix-assisted
laser
desorption
time-of-flight
mass
spectrometry
(MALDI-TOF-MS),
research
team
isolated
identified
differentially
expressed
low-abundance
samples
following
exposure
PPTT.
The
results
showed
that
there
twenty
highly
from
intervened
One
apolipoprotein
A-1
(ApoA-1)
protein,
selected
as
possible
target
explore
mechanism
action
intervention
related
signaling
pathways
involved
Hep
G2
cells.
These
findings
offer
scientifically
sound
guidance
for
further
in-depth
exploration,
development,
application
1,2,3-triazole
compound.
Molecular
mechanism
of
interaction
between
resveratrol
and
lipase
was
studied
using
fluorescence
spectroscopy
(fluorescence
spectrum,
synchronous
fluorescence,
Three-dimensional
fluorescence),
ultraviolet-visible(UV-vis)
spectroscopy,
circular
dichroic
chromatography
molecular
docking
method.
The
experiments
(The
Stern−Volmer
quenching
constants
(Ksv))
indicated
that
quenched
the
intrinsic
through
static
mechanism.
number
binding
site
about
one.
thermodynamic
functions
ΔG<0,ΔS<0
ΔH<0
process,
which
combination
process
spontaneous
exothermic
reaction
Hydrogen
bonds
van
der
Waals
forces
effect
main
force
them.
Uv-vis
spectra,
spectra
three-dimensional
analysis
showed
induced
changes
in
microenvironment
around
fluorophores
lipase,
resulting
alteration
spatial
structure
lipase.
Circular
contents
α-helix,
β-turn
β-sheet
were
decreased
of,
random
coil
increased.
All
these
experimental
results
verified
reasonably
explained
by
result.
Results
from
this
study
should
be
useful
to
elucidate
mechanisms
contribute
make
full
use
pharmaceutical
industry.
ChemistrySelect,
Journal Year:
2025,
Volume and Issue:
10(16)
Published: April 1, 2025
Abstract
Drug
interactions
with
receptors
determine
their
biological
activity.
Among
the
proteins,
human
serum
albumin
(HSA)
is
most
commonly
used
as
model
protein
to
explore
such
interactions.
The
heterocyclic
molecule,
2‐(4‐aminophenyl)
benzothiazole
(APB),
known
have
various
potential.
binding
of
APB
HSA
has
been
presented
by
looking
into
parameters
and
effect
on
structural
aspect
protein.
constant
(K
b
),
number
sites
(n),
quenching
SV
bimolecular
(k
q
)
estimated
from
experimental
spectroscopic
methods.
was
found
be
in
order
10
5
M
−1
.
Quenching
fluorescence
at
303,
308,
313
K
showed
a
dynamic
nature
quenching.
spontaneous
negative
free
energy
change
(ΔG
0
).
binding's
enthalpy
(ΔH0)
entropy
(ΔS0)
changes
suggested
significant
role
electrostatic
force.
Site‐specific
marker
displacement
studies
revealed
subdomain
IIA.
Circular
dichroism
(CD)
no
visible
HSA.
finding
corroborated
molecular
docking
that
location
This
study
may
help
understand
its
analogues
or
related
structures
aid
designing
molecules
better
Journal of Separation Science,
Journal Year:
2025,
Volume and Issue:
48(1)
Published: Jan. 1, 2025
ABSTRACT
A
comprehensive
strategy,
including
spectroscopic,
molecular
simulation,
proteomics,
and
bioinformatics
techniques,
was
employed
to
investigate
a
novel
triazole,
5‐(4‐methoxyphenyl)‐1‐phenyl‐1H‐1,2,3‐triazole,
its
interactions
with
high‐abundance
blood
proteins,
identification
of
low‐abundance
proteins.
The
binding
constants
thermodynamic
parameters
the
triazole
two
globular
human
serum
albumin,
immunoglobulin
G
(HIgG),
were
obtained
by
spectroscopic
techniques
computational
chemistry.
two‐dimensional
gel
electrophoresis
in
combination
matrix‐assisted
laser
desorption/ionization
time‐of‐flight
mass
spectrometry
isolate
identify
differentially
expressed
proteins
samples
following
exposure
triazole.
results
indicated
that
there
is
strong
albumin/HIgG
hydrophobic
interaction
plays
main
role
system.
There
21
highly
identified
from
intervened
By
analysis,
one
differential
kininogen‐1
protein,
explore
mechanism
action
5‐(4‐methoxyphenyl)‐1‐phenyl‐1H‐1,2,3‐triazole
intervention
on
kallikrein–kinin
signaling
pathways
related
HeLa
cervical
cancer
cells.
displayed
antiproliferative
activity
significantly
altered
kallikrein‐10
expression,
suggesting
possible
antitumor
involving
These
research
findings
provide
scientific
insights
for
further
development
application
1,2,3‐triazole
compound.
study
highlights
potential
compound
as
multifunctional
pharmaceutical
agent,
particularly
therapies,
lays
foundation
future
clinical
applications
targeting
drug–protein
interactions.
ChemistrySelect,
Journal Year:
2024,
Volume and Issue:
9(35)
Published: Sept. 12, 2024
Abstract
The
interaction
between
linamarin
(LIN),
a
cyanogenic
glycoside,
and
human
serum
albumin
(HSA)
was
studied
by
multiple
spectroscopic
techniques
molecular
docking
simulation.
All
measurements
were
performed
under
physiological
conditions.
obtained
results
(including
the
binding
constants,
effective
quenching
constant
number
of
sites)
showed
that
complex
HSA‐LIN
is
formed.
values
Stern‐Volmer
constants
(6.70×10
3
,
5.53×10
1.95×10
)
indicate
fluorescence
HSA
static.
Results
site
marker
experiments
LIN
mainly
located
in
I
(subdomain
IIA)
HSA.
thermodynamic
parameters
process
occurs
spontaneously
through
hydrophobic
interactions.
Molecular
are
good
agreement
with
experimental
data.
Furthermore,
computational
revealed
binds
cavity
TRP
214,
is,
subdomain
IIA
(site
I)
This
comprehensive
study
provides
deeper
insight
into
ligand
which
may
be
useful
drug
design
pharmacology.
