α-Synuclein (α-syn) amyloid fibrils are the major component of Lewy bodies, which are the pathological hallmark of Parkinson's disease (PD) and other synucleinopathies. High-resolution structure of α-syn fibril is important for understanding its assembly and pathological mechanism. Here, we determined a fibril structure of full-length α-syn (1-140) at the resolution of 3.07 Å by cryo-electron microscopy (cryo-EM). The fibrils are cytotoxic, and transmissible to induce endogenous α-syn aggregation in primary neurons. Based on the reconstructed cryo-EM density map, we were able to unambiguously build the fibril structure comprising residues 37-99. The α-syn amyloid fibril structure shows two protofilaments intertwining along an approximate 2 screw axis into a left-handed helix. Each protofilament features a Greek key-like topology. Remarkably, five out of the six early-onset PD familial mutations are located at the dimer interface of the fibril (H50Q, G51D, and A53T/E) or involved in the stabilization of the protofilament (E46K). Furthermore, these PD mutations lead to the formation of fibrils with polymorphic structures distinct from that of the wild-type. Our study provides molecular insight into the fibrillar assembly of α-syn at the atomic level and sheds light on the molecular pathogenesis caused by familial PD mutations of α-syn.

Smart textiles that sense, interact and adapt to environmental stimuli have provided exciting new opportunities for a variety of applications. However, current advances have largely remained at the research stage due to the high cost, complexity of manufacturing and This article is protected by copyright. All rights reserved.3 uncomfortableness of environmental-sensitive materials. In contrast, natural textile materials are more attractive for smart textile due to their merits in terms of low cost and comfortability. Here, we report water-fog and humidity-driven torsional and tensile actuation of thermally-set twisted, coiled, plied silk fibers, and weave textiles from these silk fibers. When exposed to water fog, the torsional silk fiber provides a fully-reversible torsional stroke of 547° mm  . Coiled-and-thermoset silk yarns provide a 70% contraction when the relative humidity (RH) is changed from 20% to 80%. Such an excellent actuation behavior originates from water absorption-induced loss of hydrogen bonds within the silk proteins and the associated structural transformation, which are corroborated by atomistic and macroscopic characterization of silk and molecular dynamics simulations. With large abundance, cost-effective, and comfortability for wearing, the silk muscles will open up more possibility in industrial applications, such as smart textiles and soft robotics.

Higher efficiency, lower cost refrigeration is needed for both large and small scale cooling. Refrigerators using entropy changes during cycles of stretching or hydrostatically compression of a solid are possible alternatives to the vapor-compression fridges found in homes. We show that high cooling results from twist changes for twisted, coiled, or supercoiled fibers, including those of natural rubber, NiTi, and polyethylene fishing line. By using opposite chiralities of twist and coiling, supercoiled natural rubber fibers and coiled fishing line fibers result that cool when stretched. A demonstrated twistbased device for cooling flowing water provides a high cooling energy and device efficiency. Theory describes the axial and spring index dependencies of twist-enhanced cooling and its origin in a phase transformation for polyethylene fibers.Summary: Twist-exploiting mechanocaloric cooling is demonstrated for rubber fibers, fishing line fibers, and NiTi shape-memory wires.3

Amyloid aggregation of α-synuclein (α-syn) is closely associated with Parkinson's disease (PD) and other synucleinopathies. Several single amino-acid mutations (e.g. E46K) of α-syn have been identified causative to the early onset of familial PD. Here, we report the cryo-EM structure of an α-syn fibril formed by N-terminally acetylated E46K mutant α-syn (Ac-E46K). The fibril structure represents a distinct fold of α-syn, which demonstrates that the E46K mutation breaks the electrostatic interactions in the wild type (WT) α-syn fibril and thus triggers the rearrangement of the overall structure. Furthermore, we show that the Ac-E46K fibril is less resistant to harsh conditions and protease cleavage, and more prone to be fragmented with an enhanced seeding capability than that of the WT fibril. Our work provides a structural view to the severe pathology of the PD familial mutation E46K of α-syn and highlights the importance of electrostatic interactions in defining the fibril polymorphs.

Tensile and torsional artificial muscles from biocompatible and biodegradable materials are highly desired for soft robotics, sensors, and controllers in bio-related applications. Twisted fibers can be used to prepare tensile...