Alzheimer’s disease and related tauopathies are characterised by the pathological aggregation of the microtubule-associated protein tau into toxic oligomers and fibrils. Previous studies have shown that zinc significantly promotes and accelerates tau aggregation by binding directly to tau within its microtubule-binding repeat domains, forming complexes that enhance nucleation and fibril formation. This study investigated whether increasing zinc concentrations leads to faster tau aggregation in a dose-dependent manner. The hypothesis was that higher Zinc concentrations would accelerate tau aggregation kinetics. Aggregation was monitored using a Thioflavin (ThT) fluorescence assay. Results partially supported the hypothesis. Samples containing higher zinc concentrations reached 50% of their maximum ThT fluorescence earlier than samples with lower Zinc levels, indicating faster aggregation. These samples also exhibited shorter lag phases and reached their plateau sooner, consistent with Zinc promoting early nucleation and fibril growth. However, the 0mM Zinc condition displayed unexpected behavior. Although it plateaued relatively quickly, it did not achieve the same maximum fluorescence intensity as the Zinc-treated samples, suggesting reduced overall fibril formation. Additionally, its relatively early plateau did not fully align with a strictly linear dose-dependent trend. These findings indicate that while Zinc enhances and accelerates tau aggregation, tau can aggregate independently, and additional factors beyond zinc concentrations likely influence aggregation kinetics.