Humanity has entered the new space age: 263 global rocket launches in 2024 (83% more than 2021's 144) and over 11,400 Earth-orbiting satellites/debris in 2024 (vs. ~7,800 in 2021) pose growing threats to space operations. In space, spacecraft/habitats need airtight breach repair, micro-meteoroid fracture sealing, and thermal cycling integrity; astronauts require radiation shielding, wound closure, and spacesuit tear repair. These demands call for materials with vacuum adhesion, hydrogel-like sealing/flexibility, strength, air/watertightness, light weight, and biocompatibility---without them, mission success and astronaut safety are at risk.
Hagfish: thread-like proteins form protective hydrogels; key HIF (α/γ) crosslink into hydrogel backbones when mixed.
Mussels: MFPs (firm wet adhesion, mfp-3b/5 critical) have wide adhesion, strength, bio-affinity (used as adhesives/coatings).
For synthetic biology production, the coding cassette is expressed in E. coli BL21(DE3) under a T7 promoter (regulated by LacI, induced by IPTG), with a 10× His-tag fused to the N-terminus for purification; post-fermentation, bacteria are harvested and lysed, and target proteins are purified via Ni-NTA affinity chromatography (IMAC).
We aim to use synthetic biology's "microbial factory" method: engineered E. coli make proteins for fast-forming adhesive hydrogels. No petroleum/large Earth supply chains; just simple carbs for in-situ mission-critical material production.
Our goals: design synthetic proteins (hydrogel properties, strength, resilience) for spacecraft/spacesuit repair; enable in-situ production with a portable fermenter (long-term missions); test in extreme space-like conditions; inspire synthetic biology for space.
In protein engineering, we designed fusion proteins by linking hagfish IF proteins (α/γ) with mfp3b/5 via a 10-aa linker---endowing the resulting hydrogels with adhesiveness for versatile use---and noted hagfish IF proteins have a tripartite structure (N-terminal "head", central α-helical CRD that facilitates α/γ heterodimerization via coiled-coils to boost slime thread mechanical properties, C-terminal "tail"); we also plan to study structure-property relationships by removing one domain, using PCR to obtain target sequences and Gibson assembly to build new coding sequences.
For application assessments, to test the engineered proteins as space-grade materials, we designed application-focused tests: comparing fusion protein variants to evaluate modular properties, testing self-assembly of proteins/mixtures into stable hydrogels, measuring adhesive strength under diverse conditions, and subjecting materials to simulated extreme environments (e.g., high/low temperatures) to assess stability and functionality---all to verify feasibility for space exploration.