Preparation and Properties of Opaque Polyethylene Terephthalate/TiO2 Filaments

The opaque polyethylene terephthalate (PET) filaments with different mass fractions of TiO2 particles were prepared by low-speed melt spinning and drafting. Basic structures including surface morphology, linear density, orientation degree and crystallinity, and properties including tensile and optical property of the PET/TiO2 filaments were systematically analyzed, especially the visual shielding property. The results showed that TiO2 particles were well-distributed on the filament surface without obvious aggregation, except when the mass fraction of TiO2 exceeded 6%. The addition of TiO2 increased the linear density of the PET filaments. The orientation degree of the filaments was positively correlated with the drafting ratio but hardly influenced by the mass fraction of TiO2. The crystallinity achieved the maximum when the mass fraction of TiO2 was 3% and then decreased gradually. The tenacity of the filaments reduced and the elongation at break enhanced initially and then decreased with the increasing TiO2 content. The opaque effect of the PET filaments improved significantly when the mass fraction of TiO2 was less than 6%, whereas the improvement of the opaque effect slowed down as the mass fraction of TiO2 increased further.

Open Source Filament Diameter Sensor for Recycling, Winding and Additive Manufacturing Machines

To overcome the challenge of upcycling plastic waste into 3D printing filament in the distributed recycling and additive manufacturing systems, this study designs, builds, tests and validates an open source 3D filament diameter sensor for recycling and winding machines. The modular system for multi-axis optical control of diameter of recycled 3D-printer filament makes it possible to analyze the surface structure of the processed filament, save the history of measurements along the entire length of the spool, as well as mark defective areas. The sensor is developed as an independent module and integrated into recyclebots. It was tested on different kinds of polymers, different sources of plastic and different colors including clear plastic. The results were compared with the manual measurements, and the measurements obtained with a one-dimensional digital light caliper. The results found that the developed open source filament sensing method allows users to obtain significantly more information in comparison with basic one-dimensional light sensors and using the received data not only for more accurate diameter measurements, but also for a detailed analysis of the recycled filament surface. The developed method ensures greater availability of plastics recycling technologies and stimulates the growth of composite materials creation. The presented system can greatly enhance the user possibilities and serve as a starting point for a complete recycling control system that will regulate motor parameters to achieve the desired filament diameter with acceptable deviations and even control the extrusion rate on a printer to recover from filament irregularities.

TNNT2mutations in the tropomyosin binding region of TNT1 disrupt its role in contractile inhibition and stimulate cardiac dysfunction

Muscle contraction is regulated by the movement of end-to-end-linked troponin−tropomyosin complexes over the thin filament surface, which uncovers or blocks myosin binding sites along F-actin. The N-terminal half of troponin T (TnT), TNT1, independently promotes tropomyosin-based, steric inhibition of acto-myosin associations, in vitro. Recent structural models additionally suggest TNT1 may restrain the uniform, regulatory translocation of tropomyosin. Therefore, TnT potentially contributes to striated muscle relaxation; however, the in vivo functional relevance and molecular basis of this noncanonical role remain unclear. Impaired relaxation is a hallmark of hypertrophic and restrictive cardiomyopathies (HCM and RCM). Investigating the effects of cardiomyopathy-causing mutations could help clarify TNT1’s enigmatic inhibitory property. We tested the hypothesis that coupling of TNT1 with tropomyosin’s end-to-end overlap region helps anchor tropomyosin to an inhibitory position on F-actin, where it deters myosin binding at rest, and that, correspondingly, cross-bridge cycling is defectively suppressed under diastolic/low Ca2+conditions in the presence of HCM/RCM lesions. The impact of TNT1 mutations onDrosophilacardiac performance, rat myofibrillar and cardiomyocyte properties, and human TNT1’s propensity to inhibit myosin-driven, F-actin−tropomyosin motility were evaluated. Our data collectively demonstrate that removing conserved, charged residues in TNT1’s tropomyosin-binding domain impairs TnT’s contribution to inhibitory tropomyosin positioning and relaxation. Thus, TNT1 may modulate acto-myosin activity by optimizing F-actin−tropomyosin interfacial contacts and by binding to actin, which restrict tropomyosin’s movement to activating configurations. HCM/RCM mutations, therefore, highlight TNT1’s essential role in contractile regulation by diminishing its tropomyosin-anchoring effects, potentially serving as the initial trigger of pathology in our animal models and humans.

Synchronized oscillations, metachronal waves, and jammed clusters in sterically interacting active filament arrays

Autonomous active, elastic filaments that interact with each other to achieve cooperation and synchrony underlie many critical functions in biology. A striking example is ciliary arrays in the mammalian respiratory tract; here individual filaments communicate through direct interactions and through the surrounding fluid to generate metachronal traveling waves crucial for mucociliary clearance. The mechanisms underlying this collective response and the essential ingredients for stable synchronization remain a mystery. In this article, we describe Brownian dynamics simulations of multi-filament arrays, demonstrating that short-range steric inter-filament interactions and surface-roughness are sufficient to generate a rich variety of collective spatiotemporal oscillatory, traveling and static patterns. Starting from results for the collective dynamics of two- and three-filament systems, we identify parameter ranges in which inter-filament interactions lead to synchronized oscillations. We then study how these results generalize to large one-dimensional arrays of many interacting filaments. The phase space characterizing the multi-filament array dynamics and deformations exhibits rich behaviors, including oscillations and traveling metachronal waves, depending on the interplay between geometric spacing between filaments, activity, and elasticity of the filaments. Interestingly, the existence of metachronal waves is nonmonotonic with respect to the inter-filament spacing. We also find that the degree of filament surface roughness significantly affects the dynamics — roughness on scales comparable to the filament thickness generates a locking-mechanism that transforms traveling wave patterns into statically stuck and jammed configurations. Our simulations suggest that short-ranged steric inter-filament interactions are sufficient and perhaps even critical for the development, stability and regulation of collective patterns.

The myosin interacting-heads motif present in live tarantula muscle explains tetanic and posttetanic phosphorylation mechanisms

Striated muscle contraction involves sliding of actin thin filaments along myosin thick filaments, controlled by calcium through thin filament activation. In relaxed muscle, the two heads of myosin interact with each other on the filament surface to form the interacting-heads motif (IHM). A key question is how both heads are released from the surface to approach actin and produce force. We used time-resolved synchrotron X-ray diffraction to study tarantula muscle before and after tetani. The patterns showed that the IHM is present in live relaxed muscle. Tetanic contraction produced only a very small backbone elongation, implying that mechanosensing—proposed in vertebrate muscle—is not of primary importance in tarantula. Rather, thick filament activation results from increases in myosin phosphorylation that release a fraction of heads to produce force, with the remainder staying in the ordered IHM configuration. After the tetanus, the released heads slowly recover toward the resting, helically ordered state. During this time the released heads remain close to actin and can quickly rebind, enhancing the force produced by posttetanic twitches, structurally explaining posttetanic potentiation. Taken together, these results suggest that, in addition to stretch activation in insects, two other mechanisms for thick filament activation have evolved to disrupt the interactions that establish the relaxed helices of IHMs: one in invertebrates, by either regulatory light-chain phosphorylation (as in arthropods) or Ca2+-binding (in mollusks, lacking phosphorylation), and another in vertebrates, by mechanosensing.

Side-binding proteins modulate actin filament dynamics

Actin filament dynamics govern many key physiological processes from cell motility to tissue morphogenesis. A central feature of actin dynamics is the capacity of filaments to polymerize and depolymerize at their ends in response to cellular conditions. It is currently thought that filament kinetics can be described by a single rate constant for each end. In this study, using direct visualization of single actin filament elongation, we show that actin polymerization kinetics at both filament ends are strongly influenced by the binding of proteins to the lateral filament surface. We also show that the pointed-end has a non-elongating state that dominates the observed filament kinetic asymmetry. Estimates of flexibility as well as effects on fragmentation and growth suggest that the observed kinetic diversity arises from structural alteration. Tuning elongation kinetics by exploiting the malleability of the filament structure may be a ubiquitous mechanism to generate a rich variety of cellular actin dynamics.

A way to identify archaellins in Halobacterium salinarum archaella by FLAG-tagging

In the current study, haloarchaea Halobacterium salinarum cells were transformed individually with each of the modified archaellin genes (flaA1, flaA2 and flaB2) containing an oligonucleotide insert encoding the FLAG peptide (DYKDDDDK). The insertion site was selected to expose the FLAG peptide on the archaella filament surface. Three types of transformed cells synthesizing archaella, containing A1, A2, or B2 archaellin modified with FLAG peptide were obtained. Electron microscopy of archaella has demonstrated that in each case the FLAG peptide is available for the specific antibody binding. It was shown for the first time that the B2 archaellin, like archaellins A1 and A2, is found along the whole filament length.