Abstract
The inhibitory effects of anti-bodies to nonphosphorylated and phosphorylated tau 441 were evaluated in vitro for aggregation, phosphorylation and microtubule stability. To evaluate inhibition of aggregation and aggregate clearance, transmission electron microscopy and fluorescence spectroscopy were used. The pSer199 levels were measured by Western blotting. The microtubule polymerization and stability was probed by fluorescence assay. Targeting the epitopes in R1 or R4 repeat domains modulated aggregation and promoted disaggregation of the preformed fibrils. Epitopes at N- and C-termini had little effect. The pSer199 level was reduced when pThr231 antibody was employed. Microtubule polymerization was reduced by several anti-tau antibodies. Epitope-targeted inhibition may be used to effectively reduce aggregation, promote disaggregation, and inhibit phosphorylation.
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