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However, these formulations face challenges such as high viscosity and elevated potential for aggregation, primarily driven by intermolecular electrostatic and hydrophobic protein\u2010protein interactions (PPIs). Achieving an acceptable injectability profile (&lt;20 cP) often necessitates the incorporation of excipients that mitigate PPIs through shielding effects. Current clinical formulations exhibit a narrow colloidal stability window, largely due to molecular changes under physical and thermal stress, whilst also suffering from suboptimal bioavailability (50%\u201385%). To address these limitations, we harness the utility of ionic liquids (ILs) that offer tunable charge and amphiphilicity profiles\u00a0as a means to simplify and stabilize protein formulations. Herein, we synthesized biocompatible choline and organic acid\u2010based ILs\u00a0and assessed their viscosity profiles with IgG antibody at both high (90 mg\/mL) and ultra\u2010high (230 mg\/mL) concentrations. Functional and structural stability assays conducted over 4 months at room temperature identified promising IL candidates for in vivo studies at both IgG concentrations. Through a multi\u2010tiered screening strategy, we generated thermally stable, ultra\u2010high concentration antibody solutions that achieved a five fold improvement in serum absorption of polyclonal IgG compared to their saline solutions.<\/jats:p>","DOI":"10.1002\/adma.202511918","type":"journal-article","created":{"date-parts":[[2026,2,5]],"date-time":"2026-02-05T05:28:23Z","timestamp":1770269303000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["High Concentration Antibody Formulations Enabled via Thermostable Ionic Liquids"],"prefix":"10.1002","volume":"38","author":[{"given":"Metecan","family":"Erdi","sequence":"first","affiliation":[{"name":"Harvard John A. 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