Protein aggregation is a major challenge encountered during manufacturing, storage and transportation of biopharmaceuticals. Aggregation of proteins is often irreversible, leading to aggregates that are inactive and potentially immunogenic; resulting in reduced efficacy and possibly toxicity of the biologic drug. Thermal stability of proteins can be improved by formulating with carbohydrates (commonly: sucrose, trehalose, and sorbitol), which prevent protein unfolding and structural loss. In our study, we investigated the stabilizing e-ffects of two ß-cyclodextrin derivatives (KLEPTOSE® HPB hydroxypropyl-ß-cyclodextrin with MS=0.65, and KLEPTOSE® HP hydroxypropyl-ß-cyclodextrin with MS=0.9), and the polyol Maltitol (a hydrogenated disaccharide), using high-throughput formulation screening (iFormulate™) and nanoDSF (Di¬erential Scanning Fluorimetry). The iFormulate™ DOE plate design provided a rapid evaluation of four critical formulation variables: pH, ionic strength, buffer concentration, and stabilizer concentration. The influence on thermal stability of two proteins, the human growth hormone (hGH) and an IgG-type therapeutic antibody (Infliximab), was evaluated under the DOE approach. Simultaneous evaluation of Tm (melting temperature) and relative degree of aggregation of proteins, with increasing concentrations of Maltitol, KLEPTOSE® HPB and HP, was performed. Our study results indicate that all three carbohydrates can be effective aggregation modulators, offering a wide range of application possibilities to address process and formulation challenges.