When subject to stress or external loads, most materials resist deformation. Any stable material, for instance, resists compression-even liquids. Solids also resist simple shear deformations that conserve volume. Under shear, however, most materials also have a tendency to expand in the direction perpendicular to the applied shear stress, a response that is known as positive normal stress. For example, wet sand tends to dilate when sheared, and therefore dries around our feet when we walk on the beach. In the case of simple solids, elastic rods or wires tend to elongate when subject to torsion. Here, we show that networks of semiflexible biopolymers such as those that make up both the cytoskeleton of cells and the extracellular matrix exhibit the opposite tendency: when sheared between two plates, they tend to pull the plates together. We show that these negative normal stresses can be as large as the shear stress and that this property is directly related to the nonlinear strain-stiffening behaviour of biopolymer gels.

Spider silk threads are formed by the irreversible aggregation of silk proteins in a spinning duct with dimensions of only a few micrometers. Here, we present a microfluidic device in which engineered and recombinantly produced spider dragline silk proteins eADF3 (engineered Araneus diadematus fibroin) and eADF4 are assembled into fibers. Our approach allows the direct observation and identification of the essential parameters of dragline silk assembly. Changes in ionic conditions and pH result in aggregation of the two proteins. Assembly of eADF3 fibers was induced only in the presence of an elongational flow component. Strikingly, eADF4 formed fibers only in combination with eADF3. On the basis of these results, we propose a model for dragline silk aggregation and early steps of fiber assembly in the microscopic regime.colloids ͉ microfluidics ͉ protein materials ͉ rheology

Fibrils or spheres? Spider silk proteins belong to the class of natively unfolded proteins. Depending on the experimental conditions, these proteins form nanofibrils or microspheres following two distinct aggregation pathways. A detailed model describes the assembly mechanism of spider silk proteins into microspheres.

Stem cell differentiation can be highly sensitive to mechanical inputs from the extracellular matrix (ECM)1–3. Identifying temporal windows during which lineage commitment responds to ECM stiffness, and the signals that mediate these decisions, would advance both mechanistic insights and translational efforts. To address these questions, we investigate adult neural stem cell (NSC) fate commitment using an oligonucleotide-crosslinked ECM platform that for the first time offers dynamic and reversible control of stiffness. “Stiffness pulse” studies in which the ECM was transiently or permanently softened or stiffened at specified initiation times and durations pinpoint a 24-hour window in which ECM stiffness maximally impacts neurogenic commitment. Overexpression of the transcriptional co-activator YAP within this window suppressed neurogenesis, and silencing YAP enhanced it. Moreover, ablating YAP-β-catenin interaction rescued neurogenesis. This work reveals that ECM stiffness dictates NSC lineage commitment by signaling via a YAP and β-catenin interaction during a defined temporal window.