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
Assistant
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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