Fibers with integrated mechanochemical switches: minimalistic design principles derived from fibronectin.

Inspired by molecular mechanisms that cells exploit to sense mechanical forces and convert them into biochemical signals, chemists dream of designing mechanochemical switches integrated into materials. Using the adhesion protein fibronectin, whose multiple repeats essentially display distinct molecular recognition motifs, we derived a computational model to explain how minimalistic designs of repeats translate into the mechanical characteristics of their fibrillar assemblies. The hierarchy of repeat-unfolding within fibrils is controlled not only by their relative mechanical stabilities, as found for single molecules, but also by the strength of cryptic interactions between adjacent molecules that become activated by stretching. The force-induced exposure of cryptic sites furthermore regulates the nonlinearity of stress-strain curves, the strain at which such fibers break, and the refolding kinetics and fraction of misfolded repeats. Gaining such computational insights at the mesoscale is important because translating protein-based concepts into novel polymer designs has proven difficult.

Running and walking with compliant legs

It has long been the dream to build robots which could walk and run with ease. To date, the stance phase of walking robots has been characterized by the use of either straight, rigid legs, as is the case of passive walkers, or by the use of articulated, kinematically-driven legs. In contrast, the design of most hopping or running robots is based on compliant legs which exhibit quite natural behavior during locomotion. © 2006 Springer.