Zamora Ramírez, William J.Campanera Alsina, Josep MariaLuque Garriga, F. Xavier2020-07-162020-07-162019-02-211948-7185https://hdl.handle.net/2445/168798Lipophilicity is a fundamental property to characterize the structure and function of proteins, motivating the development of lipophilicity scales. Here we report a versatile strategy to derive a pH-adapted scale that relies on theoretical estimates of distribution coefficients from conformational ensembles of amino acids. This is accomplished by using an accurately parametrized version of the IEFPCM/MST continuum solvation model, as an effective way to describe the partitioning between n-octanol and water, in conjunction with a formalism that combines partition coefficients of neutral and ionic species of residues, and the corresponding pKa of ionizable groups. Two weighting schemes are considered to derive solvent-like and protein-like scales, which have been calibrated by comparison with other experimental scales developed in different chemical/biological environments and pH conditions, as well as by examining properties such as the retention time of small peptides and the recognition of antigenic peptides. A straightforward extension to nonstandard residues is enabled by this efficient methodological strategy.7 p.application/pdfeng(c) American Chemical Society , 2019BioquímicaFarmacologiaBiochemistryPharmacologyinfo:eu-repo/semantics/article6910992020-07-16info:eu-repo/semantics/openAccess