Post-translational phosphorylation of the microtubule-associated protein tau is believed to have close relevance to the pathogenesis of Alzheimer's disease. The growth of amyloid fibrils of the short peptide segment VQIVY₃₁₀K (PHF6) corresponding to the core part of tau fibril formation is strongly affected by the phospholylation at Tyr310 via its electrostatic pairing with the neighboring charged lysine. Herein, we studied the propensity of resultant fibrils from PHF6 derivative peptides with charged aromatic amino acid residue at Tyr310. The results showed that the phosphorylation at Tyr310 contributed to significant enhancement of the amyloidogenicity and the stability of fibrillar aggregates. The physical origin of remarkable stabilization of fibrils by tyrosine phosphorylation is plausibly attributed to the charge pairing with the adjacent lysine residue in a similar fashion to the phosphorylation effect on the growth of amyloid fibril.