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We have searched for a minimal interaction motif in tau protein that supports the aggregation into Alzheimer-like paired helical filaments. Digestion of the repeat domain with different proteases yields a GluC-induced fragment comprising 43 residues (termed PHF43), which represents the third repeat of tau plus some flanking residues. This fragment self assembles readily into thin filaments without a paired helical appearance, but these filaments are highly competent to nucleate bona fide PHFs from full-length tau. Probing the interactions of PHF43 with overlapping peptides derived from the full tau sequence yields a minimal hexapeptide interaction motif of (306)VQIVYK(311) at the beginning of the third internal repeat. This motif coincides with the highest predicted beta-structure potential in tau. CD and Fourier transform infrared spectroscopy shows that PHF43 acquires pronounced beta structure in conditions of self assembly. Point mutations in the hexapeptide region by proline-scanning mutagenesis prevent the aggregation. The data indicate that PHF assembly is initiated by a short fragment containing the minimal interaction motif forming a local beta structure embedded in a largely random-coil protein.

proceedings of the national academy of sciences of the united states of america

Assembly of τ protein into Alzheimer paired helical filaments depends on a local sequence motif ( <sup>306</sup> VQIVYK <sup>311</sup> ) forming β structure

Assembly of τ protein into Alzheimer paired helical filaments depends on a local sequence motif ( 306 VQIVYK 311 ) forming β structure

Assembly of τ protein into Alzheimer paired helical filaments depends on a local sequence motif ( ³⁰⁶ VQIVYK ³¹¹ ) forming β structure