Abstract
Biological processes offer several intriguing examples of directed self-assembly into higher order structures that influence human health and well-being. The aggregation of microtubule associating protein Tau, an intrinsically disordered soluble protein that forms neurofibrillar tangles in cells in Alzheimer's disease may be directed by the presence of hydrophobic templates. Using various lipid monolayers and lipid-free surfaces we monitor the adsorption and aggregation kinetics of Tau proteins to these model membranes. Monitoring the surface tension change shows a two-step adsorption process followed by these proteins. A novel microrheology and quartz crystal microbalance study shows that the first step is dominated by the N-terminus of peptide, while the second step is possibly due to an intermediate hair-pin structure. Our microrheology data also show that the viscoelastic properties of these proteins is dominated by the proteins propensity to aggregate.
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