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Concentrated monoclonal antibody (mAb) solutions can lead to high viscosity as a result of protein-protein interactions and pose challenges for manufacture. Dipicolinic acid (DPA, pyridine-2,6-dicarboxylic acid) is a potential excipient for reduction of protein solution viscosity and here we describe new DPA salts with improved aqueous solubility. Crystallinity and solubility screens identified ethanolamine and diethanolamine as two promising counterions which generated crystalline, high melting point, anhydrous salt forms of DPA at 2:1 M stoichiometry. These salts significantly reduced the solution viscosity of five mAbs, equal to or better than that for the addition of arginine hydrochloride at equivalent osmolality. The presence of the DPA salts in solution did not significantly perturb the melting point of the mAbs, as determined by calorimetry, indicating an absence of any destabilization of protein conformation. Addition of the DPA salts to the mAb solutions stored at 5 °C over 6 months did not cause additional loss of the monomer fraction, though evidence of increased aggregation and fragmentation for three of the five mAbs was observed during 40 °C (accelerated and stressed) storage. Overall, this study demonstrates that ethanolamine-DPA and diethanolamine-DPA can serve as two novel excipients for viscosity reduction and could be considered by formulation scientists when developing highly concentrated mAb formulations. [ABSTRACT FROM AUTHOR]