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The microtubule‐associated protein tau participates in neurotransmission regulation via its interaction with synaptic vesicles (SVs). The precise nature and mechanics of tau's engagement with SVs, especially regarding alterations in vesicle dynamics, remain a matter of discussion. We report an electrochemical method using a synapse‐mimicking nanopipette to monitor vesicle dynamics induced by tau. A model vesicle of ~30 nm is confined within a lipid‐modified nanopipette orifice with a comparable diameter to mimic the synaptic lipid environment. Both tau and phosphorylated tau (p‐tau) present two‐state dynamic behavior in this biomimetic system, showing typical ionic current oscillation, induced by lipid‐tau interaction. The results indicate that p‐tau has a stronger affinity to the lipid vesicles in the confined environment, blocking the vesicle movement to a higher degree. Taken together, this method bridges a gap for sensing synaptic vesicle dynamics in a confined lipid environment, mimicking vesicle movement near the synaptic membrane. These findings contribute to understanding how different types of tau protein regulate synaptic vesicle motility and to underlying its functional and pathological behaviours in disease. [ABSTRACT FROM AUTHOR]

A recent article in Angewandte Chemie discusses a new method for monitoring vesicle dynamics using a synapse-mimicking nanopipette. The researchers developed a modified lipid layer within the nanopipette to mimic the lipid environment in synapses. By recording characteristic ionic current oscillations, they were able to evaluate the binding affinity of tau protein and found that phosphorylated tau inhibits vesicle dynamics through strong interactions with synaptic vesicles. This research provides valuable insights into the role of tau protein in synaptic function. [Extracted from the article]

A recent article in Angewandte Chemie International Edition discusses a new method for monitoring vesicle dynamics using a synapse-mimicking nanopipette. The researchers developed a modified lipid layer within the nanopipette to mimic the lipid environment in synapses. By recording characteristic ionic current oscillations, they were able to evaluate the binding affinity of tau protein and found that phosphorylated tau inhibits vesicle dynamics through strong interactions with synaptic vesicles. This research provides valuable insights into the role of tau protein in synaptic function. [Extracted from the article]