Dynamic thiol-disulfide exchange regulated protein assembly for adaptive and functional material design

Abstract

Achieving controlled, ordered, and dynamic protein assembly in vitro remains a major challenge in supramolecular chemistry. Dynamic thiol–disulfide exchange, a key reaction in biology, has recently emerged as a versatile and programmable tool for constructing adaptive protein-based materials. In living systems, this reversible chemistry regulates protein folding and redox balance through disulfide reshuffling between proteins and small thiols. Beyond its biological role, this mechanism provides a simple yet powerful principle for material design. Initiating protein assembly through thiol–disulfide exchange enables precise control over protein organization, allowing the creation of 0D, 1D, 2D, and 3D architectures for diverse applications such as programmable drug release systems, self-healing hydrogels and biofunctional surface coatings. This review summarizes the chemical foundation of thiol–disulfide exchange-driven protein assembly and highlights its growing potential in developing functional, adaptive protein-based materials.