PH-Dependent Conformational Plasticity of Monoclonal Antibodies at the SiO₂/Water Interface: Insights from Neutron Reflectivity and Molecular Dynamics.

ABSTRACT: Investigating the molecular conformations of monoclonal antibodies (mAbs) adsorbed at the solid/liquid interface is crucial for understanding mAb solution stability and advancing the development of mAb-based biosensors. This study examines the pH-dependent conformational plasticity of a human IgG1k mAb, COE-3, at the SiO₂/water interface under varying pH conditions (pH 5.5 and 9). By integrating neutron reflectivity (NR) and molecular dynamics (MD) simulations, we reveal that the mAb irreversibly deposits onto the interface at pH 5.5, with surface density saturation reached at 20 ppm bulk concentration. At pH 5.5, the adsorbed mAb adopts a stable "flat-on" orientation, while at pH 9, it assumes a more flexible conformation and a "tilted" orientation. This pH-dependent orientatio

SUBMITTER: Li Z 

PROVIDER: S-EPMC11672230 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature