Abstract
Tau is the major protein component of the neurofibrillary tangles that characterize a group of neurodegenerative diseases, including Alzheimers Disease. The transformation of tau from its native state where it functions as a microtubule-associated protein (MAP), to its pathological state as is found in patients suffering from any of the various associated diseases, is not well understood. Studies have shown that tau aggregation can be induced by anionic lipid vesicles, and that detergent micelles can induce folding of the microtubule binding domain of tau. Here we use fluorescence correlation spectroscopy (FCS) to monitor the interaction of tau with synthetic lipid vesicles, in order to investigate vesicle binding and aggregation. Studying several isoforms of tau, we find that solution pH plays a strong role in such interactions.
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