For more information
To learn more about the Department of Chemical Engineering at The University of South Carolina, call or mail us at:
The University of South Carolina
Department of Chemical Engineering
2C02, Swearingen Engineering Center
301 South Main Street
Columbia, SC 29208
Ph 803.777.4181
Fax 803.777.8265
Maps:
USC campus
Columbia, SC
|
 |
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 b-protein (Ab). Ab self-assembles into fibrils that deposit to yield plaques. Consequently, inhibition of Ab 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 Ab 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 Ab self-assembly processes affect both neuronal and vascular cells. In particular, Ab accumulation in the cerebrovasculature is associated with an increase in immune cell recruitment. We are interested in understanding how interactions between Ab 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
- 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).
-
Melissa A. Moss, Michael R. Nichols, Dana Kim Reed, Jan H. Hoh and Terrone L. Rosenberrry, "The peptide KLVFF-K6 promotes b-amyloid(1-40) protofibril growth by association but does not alter protofibril effects on cellular reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT)", Mol. Pharmacol. 64: 1160-1168 (2003).
-
Michael R. Nichols, Melissa A. Moss, Dana Kim Reed, Wen-Lang Lin, Rajendrani Mukhopadhyay, Jan H. Hoh and Terrone L. Rosenberry, "Growth of b-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering", Biochemistry 41: 6115-6127 (2002).
-
Melissa A. Moss and Kimberly W. Anderson, "Adhesion of cancer cells to endothelial monolayers: A study of initial attachment versus firm adhesion", J. Adhesion 74: 19-40 (2000).
-
Melissa A. Moss, Stephen Zimmer and Kimberly W. Anderson, "Role of metastatic potential in the adhesion of human breast cancer cells to endothelial monolayers", Anticancer Res. 20: 1425-1434 (2000).
|
