Self-folding nano- and micropatterned hydrogel tissue engineering scaffolds by single step photolithographic process

Current progress in tissue engineering is focused on the creation of environments in which cultures of relevant cells can adhere, grow and form functional tissue. We propose a method for controlled chemical and topographical cues through surface patterning of self-folding hydrogel films. This provides a conversion of 2D patterning techniques into a viable method of manufacturing a 3D scaffold. While similar bilayers have previously been demonstrated, here we present a faster and high throughput process for fabricating self-folding hydrogel devices incorporating controllable surface nanotopographies by serial hot embossing of sacrificial layers and photolithography

Self-folding shape memory laminates for automated fabrication

Nature regularly uses self-folding as an efficient approach to automated fabrication. In engineered systems, however, the use of self-folding has been primarily restricted to the assembly of small structures using exotic materials and/or complex infrastructures. In this paper we present three approaches to the self-folding of structures using low-cost, rapid-prototyped shape memory laminates. These structures require minimal deployment infrastructure, and are activated by light, heat, or electricity. We compare the fabrication of a fundamental structure (a cube) using each approach, and test ways to control fold angles in each case. Finally, for each self-folding approach we present a unique structure that the approach is particularly suited to fold, and discuss the advantages and disadvantages of each approach.National Science Foundation (U.S.) (Award CCF-1138967)National Science Foundation (U.S.) (Award EFRI-1240383

Optimal face-to-face coupling for fast self-folding kirigami

Kirigami-inspired designs can enable self-folding three-dimensional materials from flat, two-dimensional sheets. Hierarchical designs of connected levels increase the diversity of possible target structures, yet they can lead to longer folding times in the presence of fluctuations. Here, we study the effect of rotational coupling between levels on the self-folding of two-level kirigami designs driven by thermal noise in a fluid. Naturally present due to hydrodynamic resistance, we find that optimization of this coupling as control parameter can significantly improve a structure's self-folding rate and yield

Bi-Directional Origami-Inspired SMA Folding Microactuator

We present the design, fabrication, and characterization of single and antagonistic SMA microactuators allowing for uni- and bi-directional self-folding of origami-inspired devices, respectively. Test devices consist of two triangular tiles that are interconnected by double-beam-shaped SMA microactuators fabricated from thin SMA foils of 20 µm thickness with memory shapes set to a 180° folding angle. Bi-directional self-folding is achieved by combining two counteracting SMA microactuators. We present a macromodel to describe the engineering stress–strain characteristics of the SMA foil and to perform FEM simulations on the characteristics of self-folding and the corresponding local evolution of phase transformation. Experiments on single-SMA microactuators demonstrate the uni-directional self-folding and tunability of bending angles up to 180°. The finite element simulations qualitatively describe the main features of the observed torque-folding angle characteristics and provide further insights into the angular dependence of the local profiles of the stress and martensite phase fraction. The first antagonistic SMA microactuators reveal bi-directional self-folding in the range of −44° to +40°, which remains well below the predicted limit of ±100°

The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1)

The small G protein adenosine diphosphate ribosylation factor-1 (ARF1) is activated by cell membrane binding of a self-folding N-terminal domain. We present a model of the human ARF1 N-terminal peptide in planar lipid bilayers, determined from neutron lamellar diffraction and circular dichroism data with molecular modelling. This amphipathic domain lies at a shallow membrane depth, ideal for regulation of the ARF1 bio-timer by rapid, reversible membrane binding. The helical region does not elongate upon membrane binding, leaving the connecting flexible linker region's length unchanged.NRC publication: N