Rare Diseases Symptoms Automatic Extraction
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A random Abstract
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The effect of Alzheimer's Aβ aggregation state on the permeation of biomimetic lipid vesicles.
[gm1 gangliosidosis]
Alzheimer
's
disease
is
characterized
by
the
aggregation
and
deposition
of
the
Aβ
peptide
.
This
40
or
42
residue
peptide
is
the
product
of
the
proteolysis
of
the
amyloid
precursor
protein
membrane
protein
and
is
able
to
assemble
to
form
ordered
,
stable
amyloid
fibrils
as
well
as
small
,
soluble
,
and
potentially
cytotoxic
oligomers
.
The
toxicity
of
the
oligomers
may
be
associated
with
the
ability
to
bind
to
and
affect
the
integrity
of
lipid
membranes
.
In
this
novel
work
,
we
have
monitored
and
compared
the
ability
of
the
potent
Aβ
42
peptide
,
the
less
amyloidogenic
Aβ
40
peptide
,
and
a
variant
with
reduced
amyloidogenicity
to
bind
to
and
affect
the
integrity
of
membranes
using
dye-filled
synthetic
vesicles
.
We
reveal
that
the
potency
of
the
assemblies
reduces
with
incubation
time
of
the
peptide
and
that
maximal
effect
occurs
when
a
particular
species
is
apparent
by
electron
microscopy
.
We
have
investigated
the
effect
of
lipid
vesicle
composition
,
and
our
results
suggest
that
charge
on
the
vesicles
is
important
and
that
binding
may
partly
be
mediated
by
the
GM
1
ganglioside
receptors
expressed
in
the
outer
leaflet
of
vertebrate
membranes
.
