From the assay, a host-guest complex was inferred to have formed if there were two sets of host peaks, one from the 'empty' MOC and the other from the guest⊂MOC in slow exchange. Observation of changes in the host peak shifts were selected over changes in the guest peaks due to the aliphatic nature of many of the gueststhese guests were often found in the upfield region of the 1 H NMR spectra and therefore overlapped with solvent signals, making assignment of free and complexed guest a less viable approach in our screen. In cases where encapsulation was observed and slow-exchange is assumed, the association constant (Ka) was calculated from the integrations of host peaks relative to the host-guest peaks, assuming only a singular guest can be encapsulated (Figure , Supporting Information section S5). The calculated Ka values from this automated screen give a picture of the overall binding behavior in a MOC, informing a researcher of whether encapsulation has occurred and giving an indication of the relative strength of binding, which in turn can identify which combinations may be taken forward to perform full titrations on. Even from a relatively simple screen of 32 guests with one host, trends may be elucidated and differences in binding may direct a MOC for use in separations.