We present results of improving the OPLS-AA force field for peptides by means of refitting the key Fourier torsional coefficients. The fitting technique combines using accurate ab initio data as the target, choosing an efficient fitting subspace of the whole potential-energy surface, and determining weights for each of the fitting points based on magnitudes of the potential-energy gradient. The average energy RMS deviation from the LMP2/cc-pVTZ(-f)//HF/6-31G** data is reduced by ca. 40% from 0.81 to 0.47 kcal/mol as a result of the fitting for the electrostatically uncharged dipeptides, Transferability of the parameters is demonstrated by using the same alanine dipeptide-fitted backbone torsional parameters for all of the other dipeptides (with the appropriate side-chain refitting) and the alanine tetrapeptide. Parameters of nonbonded interactions have also been refitted for the sulfur-containing dipeptides (cysteine and methionine), and the validity of the new Coulombic charges and the van der Waals sigma 's and epsilon 's is proved through reproducing gas-phase energies of complex formation heats of vaporization and densities of pure model liquids. Moreover, a novel approach to fitting torsional parameters for electrostatically charged molecular systems has been presented and successfully tested on five dipeptides with charged side chains.