Journal of Materials Chemistry B,
Год журнала:
2024,
Номер
unknown
Опубликована: Дек. 30, 2024
In
an
antioxidant
peptide
study,
the
number
and
position
of
active
amino
acid
sites,
as
well
peptides'
conformation,
are
found
to
be
crucial
for
scavenging
hydroxyl
radicals
(˙OH).
Herein,
˙the
OH
activity
tilapia
pentapeptide
(P1,
YGDQY)
its
analogs
including
P2
(YYYGDQY),
P3
(YYGDQYY)
P4
(YYGPDQYY)
was
investigated.
The
results
showed
that
tyrosine's
amount,
location
conformation
played
important
roles
in
determining
(34.1
±
0.8%,
45.1
0.9%,
58.6
1.3%
48.4
0.96%
P1,
P2,
P3,
P4,
respectively).
Density
functional
theory
simulation
only
tyrosine
sites
located
within
effective
diffusion
distance
˙OH
could
scavenge
radical.
peptides
did
not
cause
cytotoxicity
Caco-2
cells.
And
peptide-treated
group
increase
activities
glutathione
peroxidase
(GSH-PX),
catalase
(CAT)
superoxide
dismutase
(SOD),
reduced
malondialdehyde
(MDA)
levels.
This
work
may
contribute
designing
more
based
on
natural
analogs.
Journal of Agricultural and Food Chemistry,
Год журнала:
2025,
Номер
unknown
Опубликована: Апрель 8, 2025
The
development
of
antioxidant
peptides
that
can
benefit
both
human
health
and
the
environment
is
a
major
focus
in
research.
study
aimed
to
isolate
identify
from
fermented
sea
cucumber
intestines
evaluate
their
cytoprotective
effects
against
H2O2-induced
oxidative
damage
HepG2
cells.
A
new
peptide
AAAFEGKW
(AP3)
was
obtained
through
liquid
chromatography-tandem
mass
spectrometry
virtual
molecular
docking
screening.
Synthetic
AP3
(1000
μmol/L)
demonstrated
significant
activity,
with
1,1-diphenyl-2-picrylhydrazyl,
superoxide
anion,
hydroxyl
radical
scavenging
capacities
52.99
±
1.05,
65.10
0.70,
54.17
0.85%,
respectively.
Cytoprotective
analysis
revealed
protected
oxidatively
damaged
cells
by
activating
Keap1/Nrf2
pathway,
enhancing
activities
endogenous
enzymes,
reducing
levels
reactive
oxygen
species
malondialdehyde.
Thus,
exhibits
strong
potential
as
novel
antioxidant,
making
it
suitable
for
applications
functional
foods
food
preservation.
