Salt-dependent passive adsorption of IgG1κ-type monoclonal antibodies on hydrophobic microparticles

Understanding how antibodies adsorb on solid surfaces is essential for developing effective approaches to control this process. In this study, passive adsorptions on the hydrophobic solid surface of a polystyrene microparticle (MP) of two highly similar IgG1 κ-type monoclonal antibodies (mAbs), rituximab, and trastuzumab, were examined in the presence of Hofmeister salts. Except of kosmotropic salts, the screening of electrostatic interactions using salts reduces the passive adsorption of mAbs on MP. To better understand the ion-specific adsorption process, salt-dependent Langmuir isotherm parameters were obtained and correlated for two mAbs. We find that while their maximum adsorption capacities to MPs are highly correlated (r > 0.9), the salt-dependent profiles of adsorption binding constants, K_obs, differ substantially. For rituximab, K_obs increases >10-fold in an ion-specific manner; for trastuzumab, K_obs remains constant. We conclude that even minor sequence variations among the mAbs can affect the adsorption, as well as the molecular forces attracting proteins to a solid surface. This difference might originate from the heterogeneous orientation of the adsorbed mAbs.