Melissa A. Moss
Phone 803.777.5604
Fax 803.777.8265
E-mail
3C15 Swearingen
Chemical Engineering
University of South
Carolina
301 Main St.
Columbia, SC 29208
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Melissa
A. Moss
Associate
Professor
Professor
Moss's
research
focuses
on the
problem
of Alzheimer's
disease.
One
hallmark
of Alzheimer's
disease
is the
senile
plaques
that
accumulate
in the
brain
where
they
are
associated
with
neuronal
loss
and
in the
cerebrovasculature
where
they
may
perpetuate
stoke.
These
plaques
are
composed
primarily
of the
amyloid
β-protein
(Aβ).
Aβ self-assembles
into
fibrils
that
deposit
to yield
plaques.
Consequently,
inhibition
of Aβ
self-assembly
has
emerged
as one
therapeutic
approach
for
Alzheimer's
disease.
The
focus
of our
research
is to
understand
this
self-assembly
process,
to describe
it kinetically,
and
to characterize
inhibitors
that
may
target
specific
stages
of Aβ
assembly.
We utilize
many
biophysical
techniques
including
chromatography,
fluorescence
spectroscopy,
static
and
dynamic
light
scattering,
and
atomic
force
microscopy.
Furthermore,
we seek
to determine
how
various
Aβ self-assembly
processes
affect
both
neuronal
and
vascular
cells.
In particular,
Aβ accumulation
in the
cerebrovasculature
is associated
with
an increase
in immune
cell
recruitment.
We are
interested
in understanding
how
interactions
between
Aβ and
endothelial
cells,
which
line
the
cerebrovasculature,
contribute
to an
increased
adhesion
of immune
cells
to the
cerebrovascular
endothelium.
Correlating
the
mechanism
of action
of inhibitors
with
cellular
effects
will
assist
research
efforts
to design
effective
therapeutic
agents
for
Alzheimer's
disease
therapy.
Education
- Ph. D., University of Kentucky (2000)
- B. S., University of Kentucky (1995)
Selected Publications
- F. J. Gonzalez-Velasquez, J. A. Kotarek, and M. A. Moss (2008) Soluble aggregates of the amyloid-β protein selectively stimulate permeability in human brain microvascular endothelial monolayers. In Press, Journal of Neurochemistry.
- J. A. Kotarek, K. C. Johnson, and M. A. Moss (2008) Quartz crystal microbalance analysis of growth kinetics for aggregation intermediates of the amyloid-β protein. Analytical Biochemistry, 378: 15-24.
- F. J. Gonzalez-Velasquez and M. A. Moss (2008) Soluble aggregates of the amyloid-β protein activate endothelial monolayers for adhesion and subsequent transmigration of monocyte cells. Journal of Neurochemistry, 104: 500-513.
- Melissa A. Moss, Michael R. Nichols, Dana Kim Reed, Nick Varvel and Terrone L. Rosenberry, "Nordihydroguaiaretic acid does not disaggregate β-amyloid(1-40) protofibrils but does inhibit growth arising from direct protofibril association", Mol. Pharmacol. 66: 592-600 (2004).
- Michael R. Nichols, Melissa A. Moss, Dana Kim Reed, Wen-Lang Lin, Rajendrani Mukhopadhyay, Jan H. Hoh and Terrone L. Rosenberry, "Growth of β-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering", Biochemistry 41: 6115-6127 (2002).
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