TL;DR: In this article , Zhao et al. investigated how the nanoscale forces that sustain condensates impact their stability against fusion by combining single-condensate zeta potential measurements, optical microscopy, tweezer experiments, and multiscale molecular modeling.
Abstract: Liquid-liquid phase separation underlies the formation of biological condensates. Physically, such systems are microemulsions that in general have a propensity to fuse and coalesce; however, many condensates persist as independent droplets in the test tube and inside cells. This stability is crucial for their function, but the physicochemical mechanisms that control the emulsion stability of condensates remain poorly understood. Here, by combining single-condensate zeta potential measurements, optical microscopy, tweezer experiments, and multiscale molecular modeling, we investigate how the nanoscale forces that sustain condensates impact their stability against fusion. By comparing peptide-RNA (PR25:PolyU) and proteinaceous (FUS) condensates, we show that a higher condensate surface charge correlates with a lower fusion propensity. Moreover, measurements of single condensate zeta potentials reveal that such systems can constitute classically stable emulsions. Taken together, these results highlight the role of passive stabilization mechanisms in protecting biomolecular condensates against coalescence.
TL;DR: In this paper, the adsorption characteristics of sulfonamides (SAs) on virgin MPs and aged MPs were determined under simulated conditions (ultraviolet (UV), ultraviolet combined hydrogen peroxide (UV+H2O2), and the results indicated that the surface structures of MPs changed with aging, which resulted in differences in hydrophobicity and surface charge and a significant difference in the concentrations of oxygen-containing functional groups (P).
TL;DR: The electrostatic induction of an applied voltage causes electrophoretic separation under free-flow conditions and no electrolysis or electric current flowing between the metal electrodes was observed.
Abstract: The electrostatic induction of an applied voltage causes electrophoretic separation under free-flow conditions and no electrolysis or electric current flowing between the metal electrodes was observed.
TL;DR: In this paper , the double mutant variant of SARS-CoV-2 induced conformational change in ACE2-E37, which enhanced the electrostatic interactions by the formation of a salt-bridge.
Abstract: Mutations in the receptor binding domain (RBD) in SARS-CoV-2 are shown to enhance its replication, transmissibility, and binding to host cells. Recently, a new strain is reported in India that includes a mutation (T478K, and L452R) in the RBD, that is possibly increasing the infection rate. Here, using Molecular Mechanics (MM) and Monte Carlo (MC) sampling, we show that the double mutant variant of SARS-CoV-2 induced conformational change in ACE2-E37, which enhanced the electrostatic interactions by the formation of a salt-bridge with SARS-CoV-2-R403. In addition, we observed that the double mutated structure induced a significant change in the salt-bridge electrostatic interaction between RBD-T500 and ACE2-D355. Where that this interaction lost more than 70% of its value compared to its value in WT protein.
TL;DR: It is shown that a subtle balance between electrostatic repulsion and interchain attractive interactions regulates CAPRIN1 phase separation and provides insight into how nucleotides, such as ATP, can induce formation of and subsequently dissolve protein condensates.
Abstract: Significance The surface charges of biomolecules can significantly affect how they interact with each other, including, in some cases, whether they can undergo phase separation. One example is the RNA-binding protein CAPRIN1, an important component in membraneless organelles involved in RNA processing. Focusing on the C-terminal intrinsically disordered, positively charged region of CAPRIN1, we have mapped at a residue-specific level the role of electrostatics in phase separation promoted by the addition of adenosine triphosphate. We show that the propensity of CAPRIN1 to form condensates is coupled to its neutralization and formation of intermolecular contacts. Our results highlight the interplay between repulsive electrostatic forces and favorable interchain interactions in regulating the formation of CAPRIN1 condensates.