Enhanced protein adsorption upon bulk phase separation

Adsorption, aggregation and phase separation in colloidal systems

Multivalent-Ion-Activated Protein Adsorption Reflecting Bulk Reentrant Behavior.

Protein adsorption at the solid-liquid interface is an important phenomenon that often can be observed as a first step in biological processes. Despite its inherent importance, still relatively little is known about the underlying microscopic mechanisms. Here, using multivalent ions, we demonstrate the control of the interactions and the corresponding adsorption of net-negatively charged protei...

A Concentration-Dependent Liquid Phase Separation Can Cause Toxicity upon Increased Protein Expression

Multiple human diseases are associated with a liquid-to-solid phase transition resulting in the formation of amyloid fibers or protein aggregates. Here, we present an alternative mechanism for cellular toxicity based on a concentration-dependent liquid-liquid demixing. Analyzing proteins that are toxic when their concentration is increased in yeast reveals that they share physicochemical proper...

Phase separation during freezing upon warming of aqueous solutions.

Using differential scanning calorimetry, we show that the addition of solute(s) to emulsified water lowers the freezing temperature to <231 K, the homogeneous nucleation temperature of pure bulk water, or even completely suppresses freezing. In the latter case, freezing upon warming occurs above T(X) ≈ 150 K and leads to a phase separation into pure ice and a freeze-concentrated solution (FCS) ...

Elucidating changes in interfacial water structure upon protein adsorption.

A coat to fit the body: Although protein adsorption onto surfaces is a complicated process, sum-frequency generation (SFG) spectroscopy probes the interfacial water structure around a silica surface as a model protein (bovine serum albumin, BSA) adsorbs onto it from solution. At pH 8.0, the attenuated SFG intensity after BSA adsorption indicates that interfacial water molecules are less ordered...