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As found in nature, full-length proteins consist of a genetically specified sequence of the 20 canonical amino acids, of a defined length. This sequence of chemically diverse functional groups enables the many highly controlled interactions with other molecules found in natural proteins. Recombinant proteins can be engineered to incorporate some of nature's palette of protein functionality into hydrogels for cell delivery. Current work demonstrates how this level of molecular precision can be used to address challenges in cell therapies, such as post-implantation viability, localization, and control, via specified gelation mechanics and tailored bioactive domains. Leveraging recombinant technology, including protein engineering, gene synthesis, expression, and purification, materials scientists have appropriated and modified naturally occurring proteins to achieve hydrogels that combine defined gelation mechanics with specified bioactive protein chemistries. Here, we specifically review recent developments in recombinant protein hydrogels that are either inspired by native extracellular matrix proteins (e.g. elastin, collagen, and resilin) or designed from non-matrix peptides (e.g. mixing-induced two-component hydrogels). In many of these case studies, domain- and sequence-level engineering enables a broad range of biochemical activity and mechanical control via gelation. Despite the remaining challenges of scalability and forward-designed predictability, hydrogels made of recombinant proteins offer exciting possibilities for sophisticated delivery of therapeutic cells, including multifactorial control, native-like mechanics, and sensitivity to signals from delivered cells or host tissues.

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