A Thermodynamic Analysis of the Binding Interaction Between Polysorbate 20 and 80 with Human Serum Albumins and Immunoglobulins: A Contribution to Understand Colloidal Protein Stabilisation

Patrick Garidel , Claudia Hoffmann , Alfred Blume

The development of liquid therapeutic protein drugs imposes the presence of specific stabilisation agents to prevent protein degradation in order to reach shelf-lives of at least 2 years for drugs stored at 2-8 °C. Non-ionic detergents are used to avoid protein adsorption and the formation of protein aggregates. Depending on the protein and excipient (detergent) used the stabilisation effect is quite different and can not be predicted up to now. One reason for this is the inadequate understanding of the principles that govern the stabilisation of proteins in the presence of detergents. One stabilisation mechanism discussed implicates a direct binding of detergent molecules to the hydrophobic surface area(s) of the protein in order to minimise protein-protein interactions and thus protein aggregation.

Mots clés: Calorimetry; ITC; DSC; Polysorbate; Tween; Albumin; Immunoglobulin; Antibody

Patrick Garidel, Claudia Hoffmann, Alfred Blume. A Thermodynamic Analysis of the Binding Interaction Between Polysorbate 20 and 80 with Human Serum Albumins and Immunoglobulins: A Contribution to Understand Colloidal Protein Stabilisation. Biophysical Chemistry, 2009, 143 (1-2), pp.70. ⟨10.1016/j.bpc.2009.04.004⟩. ⟨hal-00540535⟩