We describe an active polymer network in which processive molecular motors control network elasticity. This system consists of actin filaments cross-linked by filamin A (FLNa) and contracted by bipolar filaments of muscle myosin II. The myosin motors stiffen the network by more than two orders of magnitude by pulling on actin filaments anchored in the network by FLNa cross-links, thereby generating internal stress. The stiffening response closely mimics the effects of external stress applied by mechanical shear. Both internal and external stresses can drive the network into a highly nonlinear, stiffened regime. The active stress reaches values that are equivalent to an external stress of 14 Pa, consistent with a 1-pN force per myosin head. This active network mimics many mechanical properties of cells and suggests that adherent cells exert mechanical control by operating in a nonlinear regime where cell stiffness is sensitive to changes in motor activity. This design principle may be applicable to engineering novel biologically inspired, active materials that adjust their own stiffness by internal catalytic control.active soft matter ͉ cytoskeleton ͉ filamin A ͉ rheology ͉ myosin II R econstituted biopolymer networks are a class of soft material that exhibits pronounced solidlike behavior while comprising only a few percent by volume of protein. They exhibit a rich mechanical behavior and pronounced nonlinearity (1). Moreover, they model important features of living cells, because the mechanics of cells are largely controlled by a network of filamentous proteins known as the cytoskeleton. Reconstituted networks comprising one of the principal components of the cytoskeleton, filamentous actin (F-actin), are interesting models for the rheology of semiflexible polymers. Like most filamentous protein networks, they are highly responsive to external stress. Cross-linked F-actin networks exhibit strong nonlinear stiffening with strain (1, 2). This phenomenon is particularly pronounced for the case of F-actin cross-linked by filamin A (FLNa), a widely represented protein that is essential for fetal development and cell locomotion (3). FLNa is a large, highly flexible dimer that promotes orthogonal F-actin cross-linking (4). FLNa-F-actin networks are very soft in their linear regime, with shear moduli as low as 1 Pa, yet they stiffen by up to three orders of magnitude in response to external shear stress (5-8). In this respect, FLNa-F-actin resembles the behavior of living cells, which also stiffen if subjected to (tensile) stress (9, 10). Cells, however, are not passive materials, but rather use molecular motors to convert chemical energy into mechanical work within the cytoskeleton. There is evidence that cells employ internal stress generated by myosin motors to modulate their mechanics (11)(12)(13)(14)(15)(16)(17)(18)(19). This suggests a strategy of creating a new class of active materials, whose elastic properties are controlled by enzymatic activity, through addition of myosin motors to a passive F-actin network....

The absorption of light by plasmonic nanostructures and their associated temperature increase are exquisitely sensitive to the shape and composition of the structure and to the wavelength of light. Therefore, much effort is put into synthesizing novel nanostructures for optimized interaction with the incident light. The successful synthesis and characterization of high quality and biocompatible plasmonic colloidal nanoparticles has fostered numerous and expanding applications, especially in biomedical contexts, where such particles are highly promising for general drug delivery and for tomorrow’s cancer treatment. We review the thermoplasmonic properties of the most commonly used plasmonic nanoparticles, including solid or composite metallic nanoparticles of various dimensions and geometries. Common methods for synthesizing plasmonic particles are presented with the overall goal of providing the reader with a guide for designing or choosing nanostructures with optimal thermoplasmonic properties for a given application. Finally, the biocompatibility and biological tolerance of structures are critically discussed along with novel applications of plasmonic nanoparticles in the life sciences.

Cells actively produce contractile forces for a variety of processes including cytokinesis and motility. Contractility is known to rely on myosin II motors which convert chemical energy from ATP hydrolysis into forces on actin filaments. However, the basic physical principles of cell contractility remain poorly understood. We reconstitute contractility in a simplified model system of purified F-actin, muscle myosin II motors, and alpha-actinin cross-linkers. We show that contractility occurs above a threshold motor concentration and within a window of cross-linker concentrations. We also quantify the pore size of the bundled networks and find contractility to occur at a critical distance between the bundles. We propose a simple mechanism of contraction based on myosin filaments pulling neighboring bundles together into an aggregated structure. Observations of this reconstituted system in both bulk and low-dimensional geometries show that the contracting gels pull on and deform their surface with a contractile force of approximately 1 microN, or approximately 100 pN per F-actin bundle. Cytoplasmic extracts contracting in identical environments show a similar behavior and dependence on myosin as the reconstituted system. Our results suggest that cellular contractility can be sensitively regulated by tuning the (local) activity of molecular motors and the cross-linker density and binding affinity.

Absorption of electromagnetic irradiation results in significant heating of metallic nanoparticles, an effect which can be advantageously used in biomedical contexts. Also, metallic nanoparticles are presently finding widespread use as handles, contacts, or markers in nanometer scale systems, and for these purposes it is essential that the temperature increase associated with electromagnetic irradiation is not harmful to the environment. Regardless of whether the heating of metallic nanoparticles is desired or not, it is crucial for nanobio assays to know the exact temperature increase associated with electromagnetic irradiation of metallic nanoparticles. We performed direct measurements of the temperature surrounding single gold nanoparticles optically trapped on a lipid bilayer, a biologically relevant matrix. The lipid bilayer had incorporated fluorescent molecules which have a preference for either fluid or gel phases. The heating associated with electromagnetic radiation was measured by visualizing the melted footprint around the irradiated particle. The effect was measured for individual gold nanoparticles of a variety of sizes and for a variety of laser powers. The temperatures were highly dependent on particle size and laser power, with surface temperature increments ranging from a few to hundreds of degrees Celsius. Our results show that by a careful choice of gold nanoparticle size and strength of irradiating electromagnetic field, one can control the exact particle temperature. The method is easily applicable to any type of nanoparticle for which the photothermal effect is sought to be quantified.