A building‐block database of distributed polarizabilities and dipole moments to estimate optical properties of biomacromolecules in isolation or in an explicitly solvated medium

Since atomic or functional‐group properties in the bulk are generally not available from experimental methods, computational approaches based on partitioning schemes have emerged as a rapid yet accurate pathway to estimate the materials behavior from chemically meaningful building blocks. Among several applications, a comprehensive and systematically built database of atomic or group polarizabilities and related opto‐electronic quantities would be very useful not only to envisage linear or non‐linear optical properties of biomacromolecules but also to improve the accuracy of classical force fields devoted to simulate biochemical processes. In this work, we propose the first entries of such database that contains distributed polarizabilities and dipole moments extracted from fragments of peptides. Twenty three prototypical conformers of the dipeptides alanine–alanine and glycine–glycine were used to extract functional groups such as CH2, CHCH3, NH2, COOH, CONH, thus allowing construction of a diversity of chemically relevant environments. To evaluate the accuracy of our database, reconstructed properties of larger peptides containing up to six residues of alanine and glycine were tested against density functional theory calculations at the M06‐HF/aug‐cc‐pVDZ level of theory. The procedure is particularly accurate for the diagonal components of the polarizability tensor with errors up to 15%. In order to include solvent effects explicitly, the peptides were also surrounded by a box of water molecules whose distribution was optimized using the CHARMM force field. Solvent effects introduced by a classical dipole–dipole interaction model were compared to those obtained from polarizable‐continuum model calculations. A database of functional‐group polarizabilities and dipole moments is useful to envisage optical properties of biomacromolecules and to improve the accuracy of classical force fields devoted to simulate biochemical processes. Here, the first entries are extracted from fragments of dipeptides. To evaluate its accuracy, reconstructed properties of larger peptides were benchmarked against density functional theory calculations. The procedure is particularly accurate for the diagonal components of the polarizability tensor with errors up to 15%.