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However, PEGs, a carbohydrate\u2010mimicking stealth polymer, act as a macromolecular crowding agent that has a significant impact on protein aggregation depending on their concentration and molecular weight. The study systematically investigated the impact of PEG molecules with different molecular weights and concentrations on the thermal aggregation of \u03b1\u2010Lactalbumin (\u03b1\u2010LA). As the concentration was increased from 10 to 200\u2009mg\/mL of each PEG molecule (PEG6000, PEG10000, and PEG20000), the \u03b2\u2010sheet aggregates and surface hydrophobicity progressively decreased, indicating the aggregation prevention. Spectroscopic and microscopic results showed that PEGs stabilize \u03b1\u2010LA toward its native conformation, indicating the modulation of the protein surface. PEG10000 effectively showed its protective role even at its lowest concentration (10\u2009mg\/mL), suggesting its potential role in preserving protein stability and functionality. 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