This journal review article focuses on the use of assistive and rehabilitative exoskeletons as a new opportunity for individuals with diminished mobility. The article aims to identify gaps and inconsistencies in state-of-the-art assistive and rehabilitative devices, with the overall goal of promoting innovation and improvement in this field. The literature review explores the mechanisms, actuators, and sensing procedures employed in each application, specifically focusing on passive shoulder supports and active soft robotic actuator gloves. Passive shoulder supports are an excellent option for bearing heavy loads, as they enable the load to be evenly distributed across the shoulder joint. This, in turn, reduces stress and strain around the surrounding muscles. On the other hand, the active soft robotic actuator glove is well suited for providing support and assistance by mimicking the characteristics of human muscle. This review reveals that these devices improve the overall standard of living for those who experience various impairments but also encounter limitations requiring redress. Overall, this article serves as a valuable resource for individuals working in the field of assistive and rehabilitative exoskeletons, providing insight into the state of the art and potential areas for improvement.

Enzyme-induced self-assembly (EISA) is a recently developed nanotechnology technique in which small molecules are induced by cellular enzymes self-assembling into nanostructures inside cancer cells. This technique can boost the efficacy of chemotherapy drugs by avoiding drug efflux, inhibiting the cells’ DNA repair mechanisms, and targeting the mitochondria. In this work, we study the self-assembly of a short peptide and its fluorescence analogue induced by Eyes absent (EYA) tyrosine phosphatases to boost the efficacy of doxorubicin (DOX) therapy in drug-resistant types of breast cancer cells, MDA-MB-231 and MCF-7. The peptides Fmoc–FF–YP and NBD–FF–YP were synthesized with the solid-phase peptide synthesis (SPPS) method and analyzed with HPLC and MALDI-TOF. Dynamic light scattering was used to determine the size distribution of peptides exposed to the EYA enzyme in vitro. The presence of EYA enzymes in breast cancer cells was confirmed using the western blotting assay. The intracellular location of the peptide self-assembly was studied by imaging fluorescence NBD-tagged peptides. The efficacy of the peptide alone and with DOX was determined against MCF-7 and MDA-MB-231 using MTT and LIVE-DEAD assays. Nucleus and cytoplasm F-actin (Phalloidin) staining was used to determine cell morphology changes in response to the combination therapy of peptides/DOX. At an optimal concentration, the peptides are not toxic to the cells; however, they boost the efficacy of DOX against drug-resistant breast cancer cells. We used state-of-the-art computer-aided techniques to predict the molecular structure of peptides and their interactions with EYA. This study demonstrates an approach for incorporating non-cytotoxic components into DOX combination therapy, thereby avoiding increased systemic burden or adverse effects.