Lisa Lapidus, Ph.D.
Michigan State University
East Lansing, MI

Lisa Lapidus received her PhD from Harvard University in Atomic Physics in 1998. She switched her focus to biophysics by working with William Eaton at the NIH and Steven Chu at Stanford. She joined Michigan State University in 2004.

The Lapidus lab focuses on understanding the early steps of protein folding using microfluidics and laser spectroscopy, and the dynamics of unfolded proteins.  Protein aggregation is intimately related to folding since aggregation originates from unfolded or misfiled conformations (see animation and figure below).  We have shown that unfolded, aggregation-prone proteins are more likely to aggregate because they reconfigure on a slower timescale than proteins that don’t aggregate.  If a protein is reconfiguring too quickly, it does not have time to stick to another molecule before changing its conformation, but if reconfiguration and bimolecular association occur on the same timescale, aggregation is very likely.  Therefore finding molecules that can change the reconfiguration rate of the protein can prevent aggregation.  So far our lab has worked on α-synuclein (important in Parkinson’s disease) and shown that CLR01 does increase the reconfiguration rate to prevent aggregation and subsequent disease. To learn more about out study, please visit and listen to the radio report below