From Fundamental Amyloid Protein Self-Assembly to Development of Bioplastics
Tianchen Li,
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Jordan Kambanis,
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Timothy L. Sorenson
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et al.
Biomacromolecules,
Journal Year:
2023,
Volume and Issue:
25(1), P. 5 - 23
Published: Dec. 26, 2023
Proteins
can
self-assemble
into
a
range
of
nanostructures
as
result
molecular
interactions.
Amyloid
nanofibrils,
one
them,
were
first
discovered
with
regard
to
the
relevance
neurodegenerative
diseases
but
now
have
been
exploited
building
blocks
generate
multiscale
materials
designed
functions
for
versatile
applications.
This
review
interconnects
mechanism
amyloid
fibrillation,
current
approaches
synthesizing
protein-based
materials,
and
application
in
bioplastic
development.
We
focus
on
fundamental
structures
self-assembled
fibrils
how
external
factors
affect
protein
aggregation
optimize
process.
Protein
self-assembly
is
essentially
autonomous
congregation
smaller
units
larger,
organized
structures.
Since
properties
be
manipulated
by
changing
intrinsic
conditions,
serves
an
excellent
block
Building
these
principles,
general
processing
methods
pathways
from
raw
sources
mature
state
are
proposed,
providing
guide
development
large-scale
production.
Additionally,
this
discusses
diverse
nanofibrils
they
utilized
bioplastics.
The
economic
feasibility
bioplastics
also
compared
conventional
plastics
production
scenarios,
supporting
their
potential
sustainable
future
Language: Английский
Dynamic Properties of β-Casein Fibril Adsorption Layers at the Air–Water Interface
А. Р. Рафикова,
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Olga Yu. Milyaeva,
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G. Loglio
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et al.
Polymers,
Journal Year:
2025,
Volume and Issue:
17(8), P. 1075 - 1075
Published: April 16, 2025
Although
the
formation
of
layers
fibrillar
aggregates
at
liquid–liquid
and
liquid–gas
interfaces
can
significantly
increase
stability
disperse
systems,
like
foams
emulsions,
any
information
on
their
structure
properties
is
rather
limited.
In
present
work,
surface
adsorption
fibrils
intrinsically
disordered
β-casein
are
investigated.
For
unpurified
dispersions
this
protein,
dynamic
elasticity
proved
to
be
close
values
for
native
protein
solutions.
This
behavior
typical
globular
proteins.
However,
previously
studied
another
κ-casein,
do
not
demonstrate
similarity.
The
contribution
becomes
noticeable
only
after
purification
from
impurities
high
activity.
increases
up
48
mN/m
two
cycles,
i.e.,
4
times
higher
than
steady-state
same
bulk
concentrations.
Language: Английский
Mixed Adsorption Mono- and Multilayers of ß-Lactoglobulin Fibrils and Sodium Polystyrene Sulfonate
Colloids and Interfaces,
Journal Year:
2024,
Volume and Issue:
8(6), P. 61 - 61
Published: Nov. 11, 2024
The
formation
of
beta-lactoglobulin
(BLG)/sodium
polystyrene
sulfonate
(PSS)
complexes
decelerates
the
change
in
surface
properties
mixed
solutions
with
age
and
increases
steady-state
dilational
elasticity
a
narrow
PSS
concentration
range.
At
same
time,
changes
are
accelerated
dispersions
BLG
fibrils
without
due
to
influence
small
peptides
coexisting
fibrils.
A
decrease
peptide
as
result
dispersion
purification
leads
slower
at
low
concentrations.
increase
polyelectrolyte
results
an
fibril/PSS
complex
very
slow
if
exceeds
certain
critical
value.
latter
effect
is
consequence
large
aggregates
electrostatic
adsorption
barrier.
consecutive
regular
multilayers
liquid–gas
interface.
multilayer
noticeably
number
layers
from
four
six
agreement
previous
on
oppositely
charged
synthetic
polyelectrolyte,
presumably
heterogeneity
first
layer.
dynamic
approaches
250
mN/m,
indicating
that
they
can
effectively
stabilize
foams
emulsions.
Language: Английский