With the broad goal of understanding proton transfer kinetics at the ITIES, we have shown via diffusion-limited micropipette voltammetry experiments that a lipophilic basic molecule may spontaneously partition itself such that most of the observed current is carried by its conjugate acid sourced from the bulk aqueous electrolyte. We found this to be the case with 9MA as a lipophilic base and argued that any lipophilic base proceeding by this pathway for proton transfer would be unsuitable for the further study of proton-transfer kinetics. In contrast, DPP facilitated proton-transfer in micropipette electrochemical cells was found to be consistent with the expected voltammogram of interfacial proton transfer pathway, however short-lived intermediates B(aq) and HB+(aq) close to the liquid-liquid interface ultimately could not be ruled out from the experimental data. We showed with Multiphysics simulations that physically reasonable values of a neutral partitioning rate constant ( 𝑘𝑘 𝑓𝑓,𝑃𝑃ℎ𝑇𝑇 ) would lead to the suppression of the interfacial-sequential pathway over a wide range of exchange current densities considered for direct and sequential proton transfer pathways, resulting in increased confidence that the measured standard rate constant in this work is representative of interfacial direct proton transfer and not one of the other pathways considered.