Enhanced protein adsorption upon bulk phase separation.

ABSTRACT: In all areas related to protein adsorption, from medicine to biotechnology to heterogeneous nucleation, the question about its dominant forces and control arises. In this study, we used ellipsometry and quartz-crystal microbalance with dissipation (QCM-D), as well as density-functional theory (DFT) to obtain insight into the mechanism behind a wetting transition of a protein solution. We established that using multivalent ions in a net negatively charged globular protein solution (BSA) can either cause simple adsorption on a negatively charged interface, or a (diverging) wetting layer when approaching liquid-liquid phase separation (LLPS) by changing protein concentration (c_p) or temperature (T). We observed that the water to protein ratio in the wetting layer is substantially l

SUBMITTER: Fries MR 

PROVIDER: S-EPMC7316800 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature