Lihi Adler‐Abramovich

Wearable pressure sensors have become increasingly popular for personal healthcare and motion detection applications due to recent advances in materials science and functional nanomaterials. In this study, a novel composite hydrogel is presented as a sensitive piezoresistive sensor that can be utilized for various biomedical applications, such as wearable skin patches and integrated artificial skin that can measure pulse and blood pressure, as well as monitor sound as a self‐powered microphone. The hydrogel is composed of self‐assembled short peptides containing aromatic, positively‐ or negatively charged amino acids combined with 2D Ti 3 C 2 T z MXene nanosheets. This material is low‐cost, facile, reliable, and scalable for large areas while maintaining high sensitivity, a wide detection range, durability, oxidation stability, and biocompatibility. The bioinspired nanostructure, strong mechanical stability, and ease of functionalization make the assembled peptide‐based composite MXene‐hydrogel a promising and widely applicable material for use in bio‐related wearable electronics.

Redox–enzyme‐mediated electrochemical processes such as hydrogen production, nitrogen fixation, and CO 2 reduction are at the forefront of the green chemistry revolution. To scale up, the inefficient two‐dimensional (2D) immobilization of redox enzymes on working electrodes must be replaced by an efficient dense 3D system. Fabrication of 3D electrodes was demonstrated by embedding enzymes in polymer matrices. However, several requirements, such as simple immobilization, prolonged stability, and resistance to enzyme leakage, still need to be addressed. The study presented here aims to overcome these gaps by immobilizing enzymes in a supramolecular hydrogel formed by the self‐assembly of the peptide hydrogelator fluorenylmethyloxycarbonyl‐diphenylalanine. Harnessing the self‐assembly process avoids the need for tedious and potentially harmful chemistry, allowing the rapid loading of enzymes on a 3D electrode under mild conditions. Using the [FeFe] hydrogenase enzyme, high enzyme loads, prolonged resistance against electrophoresis, and highly efficient hydrogen production are demonstrated. Further, this enzyme retention is shown to arise from its interaction with the peptide nanofibrils. Finally, this method is successfully used to retain other redox enzymes, paving the way for a variety of enzyme‐mediated electrochemical applications.