Therapeutic Advantages of Nanoparticle-Impregnated Lysozyme Conjugates toward Amyloid-β Fibrillation and Antimicrobial Activity
The Journal of Physical Chemistry B,
Год журнала:
2025,
Номер
unknown
Опубликована: Янв. 15, 2025
The
interaction
of
protein
with
nanoparticles
(NPs)
varying
shape
and/or
size
boosts
our
understanding
on
their
bioreactivity
and
establishes
a
comprehensive
database
for
use
in
medicine,
diagnosis,
therapeutic
applications.
present
study
explores
the
between
lysozyme
(LYZ)
different
NPs
like
graphene
oxide
(GO)
zinc
(ZnO)
having
various
shapes
(spherical,
's',
rod-shaped,
'r')
sizes,
focusing
binding
dynamics
subsequent
effects
both
fibrillation
antimicrobial
properties.
Typically,
GO
is
considered
promising
medium
due
to
its
apparent
inhibition
prolonged
lag
phase
LYZ
fibrillation.
However,
results
showed
that
spherical
ZnO
(sZnO)
offer
superior
efficacy
modulating
an
extended
time
about
158.70
h,
further
emphasizing
importance
detailed
investigation
nanomaterial
characteristics
fibril
formation
kinetics
beyond
initial
observations.
experimental
findings
confirmed
strong
correlation
affinity
native
effective
denaturation,
ultimately
preventing
formation.
Interestingly,
nanoconjugates
intriguing
bactericidal
effects,
as
through
agar
plate
assay
SEM
imaging,
over
protein.
Overall,
this
shows
appropriate
bionanomaterials
can
exhibit
multifunctional
properties,
which
paves
way
deeper
NP
characteristics,
benefiting
wide
array
research.
Язык: Английский
Melatonin regulation of phase separation in Neuro-PASC: out-maneuvering Janus-faced amyloids
Exploration of neuroscience,
Год журнала:
2025,
Номер
4
Опубликована: Март 24, 2025
The
SAR-CoV-2
virus
has
evolved
to
co-exist
with
human
hosts,
albeit
at
a
substantial
energetic
cost
resulting
in
post-infection
neurological
manifestations
[Neuro-post-acute
sequelae
of
SARS-CoV-2
infection
(PASC)]
that
significantly
impact
public
health
and
economic
productivity
on
global
scale.
One
the
main
molecular
mechanisms
responsible
for
development
Neuro-PASC,
individuals
all
ages,
is
formation
inadequate
proteolysis/clearance
phase-separated
amyloid
crystalline
aggregates—a
hallmark
feature
aging-related
neurodegenerative
disorders.
Amyloidogenesis
during
viral
persistence
natural,
inevitable,
protective
defense
response
exacerbated
by
SARS-CoV-2.
Acting
as
chemical
catalyst,
accelerates
hydrophobic
collapse
heterogeneous
nucleation
amorphous
amyloids
into
stable
β-sheet
aggregates.
clearance
aggregates
most
effective
slow
wave
sleep,
when
high
levels
adenosine
triphosphate
(ATP)—a
biphasic
modulator
biomolecular
condensates—and
melatonin
are
available
solubilize
removal.
dysregulation
mitochondrial
dynamics
SARS-CoV-2,
particular
fusion
fission
homeostasis,
impairs
proper
distinct
subpopulations
can
remedy
challenges
created
diversion
substrates
away
from
oxidative
phosphorylation
towards
glycolysis
support
replication
maintenance.
subsequent
reduction
ATP
inhibition
synthesis
sleep
results
incomplete
brain
aggregates,
leading
commonly
associated
age-related
Exogenous
not
only
prevents
dysfunction
but
also
elevates
production,
effectively
augmenting
solubilizing
effect
moiety
ensure
timely,
optimal
disaggregation
pathogenic
prevention
attenuation
Neuro-PASC.
Язык: Английский
Pore Formation by Amyloid-like Peptides: Effects of the Nonpolar–Polar Sequence Pattern
ACS Chemical Neuroscience,
Год журнала:
2024,
Номер
15(18), С. 3354 - 3362
Опубликована: Авг. 22, 2024
One
of
the
mechanisms
accounting
for
toxicity
amyloid
peptides
in
diseases
like
Alzheimer's
and
Parkinson's
is
formation
pores
on
plasma
membrane
neurons.
Here,
we
perform
unbiased
all-atom
simulations
full
damaging
pathway,
which
includes
adsorption,
aggregation,
perforation
lipid
bilayer
pore-like
structures.
Simulations
are
performed
using
four
made
with
same
amino
acids.
Differences
nonpolar–polar
sequence
pattern
these
prompt
them
to
adsorb
into
extended
conformations
oriented
either
parallel
[peptide
labeled
F1,
Ac-(FKFE)2-NH2],
perpendicular
(F4,
Ac-FFFFKKEE-NH2),
or
an
intermediate
orientation
(F2,
Ac-FFKKFFEE-NH2,
F3,
Ac-FFFKFEKE-NH2)
regard
surface.
At
water–lipid
interface,
only
F1
fully
self-assembles
β-sheets,
F2
partially
fold
α-helical
structure.
The
β-sheets
emerge
as
electrostatic
interactions
attract
neighboring
distances
where
nonpolar
side
chains
can
interact
within
dry
core
bilayer.
This
complex
interplay
between
not
observed
other
peptides.
Although
mostly
membrane,
some
their
edges
penetrate
deep
inside
bilayer,
dragging
water
molecules
them.
precedes
pore
formation,
starts
flow
two
layers
through
that
expand
a
stable
cylindrical
delimited
by
polar
faces
spanning
both
leaflets
Язык: Английский