Research

Under the guidance of Prof. Jin Ryoun Kim, Michael is developing a peptide probe for the rapid detection of toxic alpha synuclein aggregates. Alpha synuclein aggregate species are known to play a key role in the pathogenesis of Parkinson's disease. However, there is much uncertainty surrounding which aggregate species is toxic. This substantiates the need for a peptide probe capable of distinguishing between the different aggregate species so that this recurring toxicity question can be addressed. Michael's probe would act as a biosensor, incorporating a functional coupling between recognition and signaling upon detection of alpha synuclein aggregates. Current detection methods, which require additional sample preparation steps during which these alpha synuclein aggregates may undergo significant conformational changes, could lead to erroneous results. At present, there are no methods which allow for rapid detection. Much effort has been spent in analyzing the structure of these alpha synuclein aggregates, of which the formation of a β-sheet structure is known to be critical. While most of the current research and focus revolves around this β-sheet structure, the linker region connecting two β-sheets has not been examined. Michael's research centers on varying this linker region in terms of conformation and flexibility and analyzing the effect that these changes have on aggregation behavior. Preliminary results, where aggregation behavior was modulated, have already been presented at an AIChE meeting in the fall of 2008.

Figure: NSF GK-12 Fellow, Michael Hernandez, prepares a protein sample for structural analysis. Secondary structure configuration of certain proteins plays a key role in the pathogenesis of neurodegenerative disorders, such as Parkinson's disease. Detection and signaling of these structural transitions is the focus of Michael's Ph.D. research.