Hydrodynamic and Thermodynamic Analysis of Pegylated Human Serum Albumin.

Covalent labeling of therapeutic drugs and proteins with polyethylene glycol (PEGylation) is an important modification for improving stability, solubility and half-life. PEGylation alters protein solution behavior through its impact on thermodynamic nonideality by increasing the excluded volume, and on hydrodynamic nonideality by increasing the frictional drag. To understand PEGylation's impact, we investigated the thermodynamic and hydrodynamic properties of a model system consisting of PEGylated human serum albumin (PEG-HSA) derivatives using analytical ultracentrifugation (AUC) and dynamic light scattering (DLS). We constructed PEG-HSA derivatives of single, linear 5K, 10K, 20K, 40K PEG chains and a single branched-chain PEG of 40K (2x20K). Sedimentation velocity (SV) experiments were analyzed using SEDANAL direct boundary fitting to extract ideal sedimentation coefficients s

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