The angle-based method offers a practical, easy-to-implement, and computationally efficient method that eliminates the need for manual parameter optimization, facilitating automated analyses across cages of different sizes, shapes, and window dimensions. In addition to host-guest size complementarity, guest binding is significantly influenced by electrostatic, hydrogen bonding, and Van der Waals interactions with the host, which can be significantly affected by the solvent. For example, in water, the hydrophobic effect plays a key role in driving guest binding. Ward and coworkers demonstrated that hydrophobic guests exhibit 2-3 orders of magnitude higher association constants compared to polar guests, Similarly, Ballester and coworkers established a linear relationship between binding free energies and the surface area of the non-polar guests' fragments, indicating a hydrophobic effect of 33-38 cal mol -1 Å -2 . Electrostatic complementarity is often visualized through electrostatic potential (ESP) surfaces. Molecular ESP can be calculated using ab initio methods or from charge distributions obtained by numerically solving the Poisson-Boltzmann equation or its approximate form, the generalized Born model. Additionally, hydrophobic interactions can be indirectly estimated using methods based on hydrophobic-lipophilic interactions (HLI), which quantify the tendency of nonpolar molecules to avoid contact with polar solvents, inducing aggregation and self-coiling. Another parameter, molecular hydrophobicity potential (MHP), derived from 1octanol/water partition coefficient (logP), has proven useful in describing hydrophobicity in proteins, analyzing protein pockets in docking engines, and predicting protein-ligand binding affinities. However, despite its utility in ligand-protein binding analysis, the MHP descriptor has not been commonly used to analyze cage cavities, likely due to the lack of userfriendly tools for their generation.