INFLUENCE OF SURFACTANTS UPON PROTEIN PEPTIDE ADSORPTION TO GLASS AND POLYPROPYLENE

This paper explores the use of surfactants as a pharmaceutical excipient to reduce adsorptive lasses of protein/peptide drugs. The predominant adsorption mechanism for protein/peptide drugs is shown to change with the surface and conditions of study. In the presence of surfactants, where the surfactant-surface interaction is greater than the surface-protein/peptide interaction, drug adsorption is reduced and/or eliminated. Anionic (sodium dodecyl sulfate), cationic (dodecyltrimethylammonium chloride and benzalkonium chloride) and nonionic surfactants (Polysorbate 20 and Poloxamer 188) are evaluated as possible protein/peptide adsorption controlling excipients. For protein/peptide adsorption onto glass, where an electrostatic interaction predominates, only the most hydrophobic surfactants (Polysorbate 20 and benzalkonium chloride) were significantly effective. Protein/peptide adsorption to polypropylene, where a hydrophobic/dehydration mechanism predominates, allows additional surface-active agents to be effective in reducing drug adsorption.