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

Achieving controlled, ordered, and dynamic protein assembly <i>in vitro</i> 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.