Molecular-surfactant-stabilized emulsions are susceptible to coalescence and Ostwald ripening. Amphiphilic particles, which have a much stronger anchoring strength at the interface, could effectively alleviate these problems to form stable Pickering emulsions. Herein, we describe a versatile method to fabricate biocompatible amphiphilic dimer particles through controlled coprecipitation and phase separation. The dimer particles consist of a hydrophobic PLA bulb and a hydrophilic shellac-PEG bulb, thus resembling nonionic molecular surfactants. The size and diameter ratio of the dimer particles are readily tunable, providing flexible control over the water/oil interfacial curvature and thus the type of emulsion. The particle-stabilized emulsions were stable for a long period of time and could be destabilized through a pH-triggered response. The biocompatible amphiphilic dimer particles with tunable morphology and functionality are thus ideal colloidal surfactants for various applications.
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http://dx.doi.org/10.1002/anie.202001588 | DOI Listing |
PLoS Pathog
January 2025
Division of Infectious Diseases, University of Colorado Anschutz Medical Campus School of Medicine, Aurora, Colorado, United States of America.
Lenacapavir (LEN) is a highly potent, long-acting antiretroviral medication for treating people infected with muti-drug-resistant HIV-1 phenotypes. The inhibitor targets multifaceted functions of the viral capsid protein (CA) during HIV-1 replication. Previous studies have mainly focused on elucidating LEN's mode of action during viral ingress.
View Article and Find Full Text PDFJ Phys Chem Lett
January 2025
University of Maryland Computer-Aided Drug Design Center, Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland 21201, United States.
An improvement in the computational efficiency of polarizable force field simulations is made through the development of a polarizable Drude water model, SWM3, in combination with the use of Lennard-Jones Particle Mesh Ewald (LJPME) for the treatment of long-range LJ interactions. The experimental bulk properties, density, heat of vaporization, dielectric constant, and self-diffusion constant of the SWM3 model are accurately replicated at ambient condition. The temperature dependence of the bulk properties is also captured except for the density.
View Article and Find Full Text PDFEnviron Sci Technol
January 2025
State Key Laboratory of Pollution Control and Resource Reuse, School of the Environment, Nanjing University, Nanjing, Jiangsu Province 210023, China.
Nanoplastics (NPs) are ubiquitous in the environment, posing significant threats to biological systems, including nervous systems, across various trophic levels. Nevertheless, the molecular mechanisms behind the size-dependent neurotoxicity of NPs remain unclear. Here, we investigated the neurotoxicity of 20 and 100 nm polystyrene NPs (PS-NPs) to zebrafish.
View Article and Find Full Text PDFJ Chem Phys
January 2025
Department of Physics and Materials Science, The University of Memphis, Memphis, Tennessee 38152, USA.
The adhesion of nanoparticles to lipid vesicles causes curvature deformations to the membrane to an extent determined by the competition between the adhesive interaction and the membrane's elasticity. These deformations can extend over length scales larger than the size of a nanoparticle, leading to an effective membrane-curvature-mediated interaction between nanoparticles. Nanoparticles with uniform surfaces tend to aggregate into unidimensionally close-packed clusters at moderate adhesion strengths and endocytose at high adhesion strengths.
View Article and Find Full Text PDFbioRxiv
January 2025
Ben-May Institute for Cancer Research, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Insulin degrading enzyme (IDE) is a dimeric 110 kDa M16A zinc metalloprotease that degrades amyloidogenic peptides diverse in shape and sequence, including insulin, amylin, and amyloid-β, to prevent toxic amyloid fibril formation. IDE has a hollow catalytic chamber formed by four homologous subdomains organized into two ~55 kDa N- and C- domains (IDE-N and IDE-C, respectively), in which peptides bind, unfold, and are repositioned for proteolysis. IDE is known to transition between a closed state, poised for catalysis, and an open state, able to release cleavage products and bind new substrate.
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