From canonical to unique: extension of a lipophilicity scale of amino acids to non-standard residues

Aim: The lipophilicity of amino acids plays a crucial role in delineating their physicochemical properties, offering insights into solubility, binding affinity, and bioavailability, properties that are a cornerstone for the use of peptides as therapeutic agents. In this study, we employ the integral equation formalism polarizable continuum model/Miertus-Scrocco-Tomasi (IEFPCM/MST) implicit solvation model to compute the n-octanol/water partition coefficient, serving as a lipophilic descriptor for non-standard amino acids. This approach allows us to expand upon our prior scale developed for canonical amino acids.