A novel colorimetric sensor to track the morphological evolution of SOD1 aggregation
S. Hong, I. Choi, J. Lee, S. Lee, Y. I. Yang, Y. Kim, K. Choi and J. Yi
Seoul National University, KR
Amyloidogenesis, Au nanoparticle, protein aggregates, superoxide dismutase (SOD1)
Amyloidogenesis is an important issue in biophysical process that has been associated with a number of human neurodegerative diseases, including Lou Gehrig’s disease, Alzheimer's disease and Parkinson's disease. One of major proteins involved in these diseases is known to be superoxide dismutase (SOD1). Up to now, the pathogenic mechanism with the association of protein aggregates has not been clearly revealed. Thus, a sensitive and precise method is required to detect the structural evolution of protein aggregates, which can provide a definitive molecular basis for the clinical laboratory diagnosis . In this study, functionalized metal nanoparticles with appropriate aggregate-tracer were progressively assembled into the SOD1 aggregate. Consequently, it provided a clue to understand pathology of SOD1-related amyotrophic lateral sclerosis (ALS). Here, we used Au nanoparticle/SOD1 complexes as a sensing probe for the detection of the morphological evolution of the SOD1 aggregation. The specific interactions between Au nanoprobe and SOD1 aggregates cause measurable shifts in the color of the SOD1-coated nanoparticle solutions detected by UV-vis absorption spectroscopy. Interestingly, dynamic distance between the particles became shorter due to the protein aggregation, thus the particles might be coaxed to function as colorimetric reporters for the structural evolution of SOD1 aggregate. This method proposed will provide a simple colorimetric tracking of the morphological evolution of SOD1 aggregation and put the first step towards a possible diagnosis of ALS.
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Nanotech 2007 Conference Program Abstract