Advanced Healthcare Materials,
Journal Year:
2025,
Volume and Issue:
unknown
Published: Jan. 6, 2025
Abstract
Neurodegenerative
diseases,
particularly
Alzheimer's
disease
and
Parkinson's
disease,
present
formidable
challenges
in
modern
medicine
due
to
their
complex
pathologies
the
absence
of
curative
treatments.
Despite
advances
symptomatic
management,
early
diagnosis
remains
essential
for
mitigating
progression
improving
patient
outcomes.
Traditional
diagnostic
methods,
such
as
MRI,
PET,
cerebrospinal
fluid
biomarker
analysis,
are
often
inadequate
detection
these
diseases.
Emerging
porous
materials,
including
metal–organic
frameworks
(MOFs),
covalent–organic
(COFs),
MXene,
zeolites,
silicon,
offer
promising
new
approaches
neurodegenerative
These
characterized
by
highly
tunable
physicochemical
properties,
have
potential
capture
concentrate
disease‐specific
biomarkers
amyloid‐beta
(Aβ),
tau
protein,
alpha‐synuclein
(α‐Syn).
The
integration
materials
into
advanced
biosensors
real‐time
holds
promise
revolutionizing
neurodiagnostic,
enabling
non‐invasive,
sensitive,
specific
platforms.
Furthermore,
incorporation
artificial
intelligence
(AI)
machine
learning
(ML)
techniques
analysis
sensor
data
enhances
accuracy
allows
more
efficient
interpretation
profiles.
AI
ML
can
optimize
feature
selection,
improve
pattern
recognition,
facilitate
prediction
progression,
making
them
indispensable
tools
personalized
medicine.
This
review
explores
diagnostics,
emphasizing
design,
functionality,
synergistic
role
advancing
clinical
applications.
Chemical Society Reviews,
Journal Year:
2020,
Volume and Issue:
49(15), P. 5473 - 5509
Published: Jan. 1, 2020
Amyloid
diseases
are
global
epidemics
with
profound
health,
social
and
economic
implications
yet
remain
without
a
cure.
This
dire
situation
calls
for
research
into
the
origin
pathological
manifestations
of
amyloidosis
to
stimulate
continued
development
new
therapeutics.
In
basic
science
engineering,
cross-β
architecture
has
been
constant
thread
underlying
structural
characteristics
functional
amyloids,
realizing
that
amyloid
structures
can
be
both
in
nature
fuelled
innovations
artificial
whose
use
today
ranges
from
water
purification
3D
printing.
At
conclusion
half
century
since
Eanes
Glenner's
seminal
study
amyloids
humans,
this
review
commemorates
occasion
by
documenting
major
milestones
date,
perspectives
biology,
biophysics,
medicine,
microbiology,
engineering
nanotechnology.
We
also
discuss
challenges
opportunities
drive
interdisciplinary
field
moving
forward.
Journal of the American Chemical Society,
Journal Year:
2019,
Volume and Issue:
141(14), P. 6092 - 6107
Published: March 20, 2019
Controlling
polymorphism
in
molecular
solids
is
of
great
interest
since
the
properties
and
performances
materials
depend
on
molecules'
mutual
packing
arrangements.
Herein,
we
describe
a
perylene
bisimide
(PBI)
organogelator
molecule
PBI-4
that
self-assembles
into
three
different
one-dimensional
supramolecular
polymorphs
(Agg
1-3)
same
solvent
at
concentration
room
temperature.
The
were
characterized
by
UV/vis,
CD,
fluorescence
IR
spectroscopy,
atomic
force
microscopy
(AFM),
theoretical
calculations,
revealing
their
arrangements
are
governed
distinct
π-π-stacking
modes
unique
hydrogen-bonding
patterns.
Nudged
elastic
band
(NEB)
calculations
for
nucleation
processes
toward
Agg
2
3
indicate
starts
from
central
kinetically
trapped
state
1
involves
reorganization
dimers.
Time-,
concentration-,
temperature-dependent
UV/vis
experiments
provided
insights
thermodynamic
stability
kinetics
interconversion.
On
basis
this
information
production
certain
polymorph
could
be
accomplished
either
physically
ultrasonication
or
chemically
seeding.
This
work
contributes
to
understanding
lowest
level
hierarchy
generation
self-assembled
1D
aggregate
structures.
Nature Communications,
Journal Year:
2019,
Volume and Issue:
10(1)
Published: May 27, 2019
Artificial
nanoparticles
accumulate
a
protein
corona
layer
in
biological
fluids,
which
significantly
influences
their
bioactivity.
As
nanosized
obligate
intracellular
parasites,
viruses
share
many
biophysical
properties
with
artificial
extracellular
environments
and
here
we
show
that
respiratory
syncytial
virus
(RSV)
herpes
simplex
type
1
(HSV-1)
rich
distinctive
different
fluids.
Moreover,
pre-coating
differentially
affects
viral
infectivity
immune
cell
activation.
In
addition,
demonstrate
bind
amyloidogenic
peptides
catalyze
amyloid
formation
via
surface-assisted
heterogeneous
nucleation.
Importantly,
HSV-1
catalyzes
the
aggregation
of
β-peptide
(Aβ
Advanced Sustainable Systems,
Journal Year:
2023,
Volume and Issue:
7(4)
Published: Jan. 12, 2023
Abstract
Artificial
functional
materials
based
on
amyloid
fibrils
are
proven
to
be
a
promising
strategy
toward
materials.
However,
scaling‐up
applications
present
sustainability
concerns,
as
animal
proteins
the
main
sources
for
fabricating
fibrils.
Plant‐protein‐based
fibrils,
more
sustainable
alternative
proteins,
attracting
increasing
interests
building
blocks
in
Herein,
11
different
from
wide
range
of
plants
evaluated,
and
comprehensive
analysis
seven
species
plant
including
kidney
bean,
black
cowpea,
mung
chickpea,
lentil,
pumpkin
seed,
with
an
excellent
ability
form
is
presented.
A
universal
diversity
protein
extraction
fibrillization
applied.
Flexible
persistence
length
≈100
nm
rigid
several
micrometers
discovered
7S/8S
11S
subunits
dominated
protein,
respectively.
Structural
evolution
β‐sheet
content
these
proteinaceous
assemblies
characterized
by
thioflavin
T
(ThT)
intensity,
circular
dichroism
(CD)
spectra,
attenuated
total
reflectance‐Fourier
transform
infrared
(ATR‐FTIR)
typical
angle
X‐ray
scattering
(WAXS)
spectra.
Finally,
their
multifunctional
further
explored
that
amyloids
demonstrate
performance
renewable
degradable
bioplastics,
water
purification
membranes
heavy
metal
removal.
Diseases,
Journal Year:
2023,
Volume and Issue:
11(1), P. 30 - 30
Published: Feb. 9, 2023
Proteins
are
central
to
life
functions.
Alterations
in
the
structure
of
proteins
reflected
their
function.
Misfolded
and
aggregates
present
a
significant
risk
cell.
Cells
have
diverse
but
integrated
network
protection
mechanisms.
Streams
misfolded
that
cells
continuously
exposed
must
be
continually
monitored
by
an
elaborated
molecular
chaperones
protein
degradation
factors
control
contain
misfolding
problems.
Aggregation
inhibition
properties
small
molecules
such
as
polyphenols
important
they
possess
other
beneficial
antioxidative,
anti-inflammatory,
pro-autophagic
help
neuroprotection.
A
candidate
with
desired
features
is
for
any
possible
treatment
development
aggregation
diseases.
There
need
study
phenomenon
so
we
can
treat
some
worst
kinds
human
ailments
related
aggregation.
Archives of Biochemistry and Biophysics,
Journal Year:
2019,
Volume and Issue:
664, P. 134 - 148
Published: Feb. 10, 2019
The
development
of
atomic
force
microscopy
(AFM)
has
opened
up
a
wide
range
novel
opportunities
in
nanoscience
and
new
modalities
observation
complex
biological
systems.
AFM
imaging
been
widely
employed
to
resolve
the
heterogeneous
conformational
states
involved
protein
aggregation
at
single
molecule
scale
shed
light
onto
molecular
basis
variety
human
pathologies,
including
neurodegenerative
disorders.
study
individual
macromolecules
nanoscale,
however,
remains
challenging,
especially
when
fully
quantitative
information
is
required.
In
this
review,
we
first
discuss
principles
with
special
emphasis
on
fundamental
factors
defining
its
sensitivity
accuracy.
We
then
review
parameters
approaches
work
limit
resolution
order
perform
statistical
analysis
biomolecules
nanoscale
aggregates.
This
approach
proved
be
powerful
unravel
hierarchical
assembly
misfolded
species
present
transiently
during
aggregation,
visualise
their
dynamics
as
well
structural
properties
amyloid-inspired
functional
nanomaterials.
Advanced Materials,
Journal Year:
2019,
Volume and Issue:
32(18)
Published: June 11, 2019
Abstract
Amyloidosis
is
a
biophysical
phenomenon
of
protein
aggregation
with
biological
and
pathogenic
implications.
Among
the
various
strategies
developed
to
date,
nanomaterials
multifunctional
nanocomposites
possessing
certain
structural
physicochemical
traits
are
promising
candidates
for
mitigating
amyloidosis
in
vitro
vivo.
The
mechanisms
underpinning
toxicity
introduced,
opportunities
materials
science
drive
this
interdisciplinary
field
forward
highlighted.
Advancement
emerging
frontier
hinges
on
exploitation
self‐assembly
interactions
amyloid
proteins
nanoparticles,
intracellular
extracellular
proteins,
chaperones,
membranes,
organelles,
biometals.