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Therapeutic implication of L-phenylalanine aggregation mechanism and its modulation by D-phenylalanine in phenylketonuria.
[phenylketonuria]
Self-assembly
of
phenylalanine
is
linked
to
amyloid
formation
toxicity
in
phenylketonuria
disease
.
We
are
demonstrating
that
L-
phenylalanine
self-assembles
to
amyloid
fibrils
at
varying
experimental
conditions
and
transforms
to
a
gel
state
at
saturated
concentration
.
Biophysical
methods
including
nuclear
magnetic
resonance
,
resistance
by
alpha-phenylglycine
to
fibril
formation
and
preference
of
protected
phenylalanine
to
self-assemble
show
that
this
behaviour
of
L-
phenylalanine
is
governed
mainly
by
hydrophobic
interactions
.
Interestingly
,
D-
phenylalanine
arrests
the
fibre
formation
by
L-
phenylalanine
and
gives
rise
to
flakes
.
These
flakes
do
not
propagate
further
and
prevent
fibre
formation
by
L-
phenylalanine
.
This
suggests
the
use
of
D-
phenylalanine
as
modulator
of
L-
phenylalanine
amyloid
formation
and
may
qualify
as
a
therapeutic
molecule
in
phenylketonuria
.
Diseases
Validation
Diseases presenting
"nuclear magnetic resonance"
symptom
homocystinuria without methylmalonic aciduria
phenylketonuria
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