Building upon our comprehensive characterization of AZD8205 biotransformation we can glean the various biochemical reactions that enable us to obtain more mechanistic understanding of ADC biotransformation pathways. This is particularly important from translational ADME point of view, as such knowledge would be important to understand the translatability of PK and PD data between animal models and the clinical setting. In addition to the known role of proteases in protein degradation, other endogenous molecules and microenvironments may influence ADC biotransformation. One avenue for interrogating the mechanisms of ADC biotransformation is by examining the endogenous molecules covalently and non-covalently associated with ADCs or their catabolites. Redox pairs such as cysteine and GSH have been observed to interact with AZD8205 and its catabolites. Further understanding of the determinants behind these interactions may provide further supporting evidence in translating these preclinical study results to patients.