Polyelectrolytes with ionic domains screened by bulky hydrophobic segments form processable, hydrophobic complexes called “compleximers”. Ionic liquids, which are chemically similar, further plasticize compleximers, yet the mechanisms behind their plasticization effects and distribution within the complexes remain unclear. This study examines the relaxation dynamics of plasticized compleximers across multiple length scales using rheology, fluorescence recovery after photobleaching (FRAP), and broadband dielectric spectroscopy (BDS). The incorporation of ionic liquids into compleximers reduces their glass transition temperature (T_g), accelerates diffusive processes, increases segmental motion, and leads to a small decrease in activation energy associated with these relaxation processes. However, the activation energies vary substantially between techniques, probing different physical processes: approximately 200 kJ/mol in rheology, 50 kJ/mol in FRAP, and 90 kJ/mol in BDS. These variations suggest that collective dynamics strongly influence the compleximer rheology, making the mobilization (and activation) of polymer chains distinct from the local movement of ionic segments.

Collagen forms the structural scaffold of connective tissues in all mammals. Tissues are remarkably resistant against mechanical deformations because collagen molecules hierarchically self-assemble in fibrous networks that stiffen with increasing strain. Nevertheless, collagen networks do fracture when tissues are overloaded or subject to pathological conditions such as aneurysms. Prior studies of the role of collagen in tissue fracture have mainly focused on tendons, which contain highly aligned bundles of collagen. By contrast, little is known about fracture of the orientationally more disordered collagen networks present in many other tissues such as skin and cartilage. Here, we combine shear rheology of reconstituted collagen networks with computer simulations to investigate the primary determinants of fracture in disordered collagen networks. We show that the fracture strain is controlled by the coordination number of the network junctions, with less connected networks fracturing at larger strains. The hierarchical structure of collagen fine-tunes the fracture strain by providing structural plasticity at the network and fiber level. Our findings imply that low connectivity and plasticity provide protective mechanisms against network fracture that can optimize the strength of biological tissues.