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

• D. D. Soto-Ortega, B. P. Murphy, F. J. Gonzalez-Velasquez, K. A. Wilson, F. Xie, Q. Wang, and M. A. Moss ( 2011 ), "Inhibition of amyloid-β aggregation by coumarin analogs can be manipulated by functionalization of the aromatic center," Bioorganic and Medicinal Chemistry, 19: 2596 - 2602
• F. J. Gonzalez-Velasquez, J. W. Reed, J. W. Fuseler, E. E. Matherly, J. A. Kotarek, D. D. Soto-Ortega, and M. A. Moss
  ( 2010 ), "Activation of brain endothelium by soluble aggregates of the amyloid-β protein involves nuclear factor‑κB," Current Alzheimer’s Research, Invited Contribution for special issue on Neuroinflammation in Alzheimer’s Dissease, 8: 91 - 94
• J. A. Kotarek and M. A. Moss ( 2010 ), "Impact of physpholipid bilayer saturation on amyloid-β aggregation intermediate growth: A quartz crystal microbalance analysis," Analytical Biochemistry, 399: 30 - 38
• T. J. Davis, D. D. Soto-Ortega, J. A. Kotarek, F. J. Gonzalez-Velasquez, K. Sivakumar, L. Wu, Q. Wang, and M. A. Moss
  ( 2009 ), "Comparative study of inhibition at multiple stages of amyloid-β self - assembly provides mechanistic insight," Molecular Pharmacology, 76: 405 - 413
• 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," Journal of Neurochemistry, 107: 466 - 477