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Jordi Folch-Pi Memorial Award for 1998

Dr. Regina M. Murphy

Dr. Regina M. Murphy

Regina Murphy was the 1998 recipient of the Jordi Folch-Pi Award for her studies on mechanisms of protein aggregation. Specifically, her research has focused on elucidating the kinetics of aggregation of amyloidogenic proteins involved in neurodegenerative disease, with particular current interests in beta-amyloid peptide and proteins with expanded polyglutamine domains. In her work she uses a number of biophysical tools such as laser light scattering, fluorescence spectroscopy, circular dichroism and mathematical models. Her interest in kinetics derives from a belief that the pathways of aggregation can only be understood by examining the kinetics in a rigorous and quantitative manner, and that the aggregation pathways are intimately linked with the mechanisms of toxicity. In some of her early work, she showed that different methods of preparing beta-amyloid samples produced markedly different aggregation kinetics, which might explain some of the wide variability observed in toxicity assays. Her lab showed that soluble oligomers of beta-amyloid formed spontaneously, early in the aggregation process, well before the appearance of mature insoluble fibrils. She developed small peptides that accelerate beta-amyloid aggregation but inhibited toxicity; this was some of the first data indicating that soluble oligomers may in fact be more toxic than insoluble fibrils. She has proceeded with structure-function studies to more precisely define the nature and mechanism of action of these peptide inhibitors, and has demonstrated a relationship between aggregation kinetics and interaction of beta-amyloid with lipid bilayers. Her lab is currently examining the interaction of transthyretin with beta-amyloid, in light of recent studies suggesting that transgenic mice mount a protective response to amyloid deposition by over-expressing transthyretin. In another project, her lab is investigating the kinetics of aggregation of polyglutamine peptides and proteins as a function of polyglutamine length and context, because of the role of these proteins in Huntington's and related neurodegenerative disease. Dr. Murphy received her Ph.D in Chemical Engineering from MIT and joined the faculty at University of Wisconsin in 1989 where she is presently a Professor. She has been the recipient of numerous other awards including the: NSF Presidential Young Investigator Award (1990); Alumni Teaching Quality Award (1992); S.C. Johnson Distinguished Fellow Award (1997); Romnes Faculty Fellow (1999) and the James G. Woodburn Award for Excellence in Teaching (2006). Her research has been supported by the American Health Assistance Foundation, the Alzheimer's Association, NIH and NSF.