Four established ReaxFF force fields, trained on biochemical systems, have been systematically benchmarked on 20 proteinogenic amino acids and 11 dipeptides. The force fields were compared with respect to geometries, energetics, and atomic charges of conformers for the amino acids. To assess the performance with respect to reactivity, the condensation reactions for the formation of dipeptides were investigated by calculating the reaction energetics and pathways. We found systematic errors in the torsion angles for the amino acids, with deviations over 100°, and a generally incorrect account of relative energies for amino acid conformers. In describing the reactivity, only one of the force fields could reproduce the reaction energies of amino acid condensations quantitatively. All four force fields predict unphysical mechanisms for these reactions, involving highly unstable intermediate structures, proton transfers involving aliphatic protons, and even five-coordinate carbon atoms. The corresponding energy landscapes exhibit fluctuations on small length scales and artificial minima.