Freeze-Induced Protein Assembly of α-Synuclein into Stable Microspheres to Fabricate Light-Induced Cargo Release Systems.

Stable hollow-type microspheres (MSs) have been fabricated using α-synuclein (αS), an amyloidogenic protein, via freeze-induced protein self-assembly. This assembly process involves three steps: rapid freezing to form spherical protein condensates from αS oligomers, frozen annealing to form a crust on the condensate and freeze-drying to create an interior lumen via the three-dimensional (3D) coffee-stain effect. The crust produced during the frozen-annealing step is a β-sheet-mediated protein structure that is presumed to be created at the quasi-liquid layer of the protein-ice interface and thus contributes to the stability of MSs in aqueous solutions at room temperature without any additional surface stabilization.

Combination of Chemical and Physical Cancer Therapeutics Developed with Microcapsules Made of κ-Casein and Gold Nanoparticles in the Presence of Drug-Loaded Phase Change Materials.

Tumor heterogeneity requires development of an anticancer system equipped with both chemical and physical therapeutics to eradicate cancer exhibiting drug resistance and clonal evolution into diverse tumor cells. Assortment of various toxic components into one platform without compromising their individual toxic activity remains a formidable task. Herein, a novel drug delivery system (DDS) exerting potent cytotoxicity toward cancer cells was fabricated with gold nanoparticles (AuNPs) coated with an innocuous self-assembly protein of κ-casein (κC).

Disulfide-Mediated Elongation of Amyloid Fibrils of α-Synuclein For Use in Producing Self-Healing Hydrogel and Dye-Absorbing Aerogel.

Due to their mechanical robustness, biocompatibility, and nanoscale size, amyloid fibrils (AFs) have been considered as a potential nanomaterial for biological applications. Unfortunately, however, AFs are usually not fully extended because of their pre-mature breakage, which hampers their use to generate biocompatible suprastructures, although the amounts of AFs could be amplified via their self-propagation property. Here, we have demonstrated the full extension of AFs of α-synuclein (αS) by introducing a cysteine residue to its C-terminus which prevents the shear-induced fragmentation of AFs via site-directed disulfide bond formation on the exposed surface of AFs.

Fabrication of a Dual Stimuli-Responsive Assorted Film Comprising Magnetic- and Gold-Nanoparticles with a Self-Assembly Protein of α-Synuclein.

Development of sensing elements for controllable soft materials is crucial to improve their responsiveness toward remotely provided external stimuli. Magnetic nanoparticles (MNPs) and gold nanoparticles (AuNPs) have been coassembled into a flexible free-floating 2D film to produce a shape deformable mobile structure in the presence of magnetic field and light irradiation by employing a self-assembly protein of α-synuclein (αS). αS was demonstrated to be essential for the preparation of a multisensory system because the intrinsically disordered protein led to a complete dispersion of MNPs to an average size of 10 nm in aqueous solution, pH-dependent closely packed single layer adsorption of αS-MNPs, and α-helix-mediated free-floating MNP monolayer film formation upon dissolving the underlying polycarbonate substrate with chloroform.