ArticleBioactive materials2026
Bioinspired silk-catechol-enzyme co-assemblies as jigsaw-designed conformation-locking bioactive-biocatalytic platforms.
Article in Bioactive materials, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Immobilized enzymes offer a sustainable, cost-effective alternative to soluble catalysis, but an adaptable platform preserving native conformation, stability, and broad enzyme/material compatibility remains elusive. We report a facile, general, jigsaw-designed platform via co-assembling silk fibroin (SF), protocatechualdehyde (PA), and enzymes. Mussel-inspired PA remodels SF into β-sheet-rich "nano-pockets" to conformationally lock bioenzymes, while its aldehyde and catechol moieties anchor enzymes and surfaces, yielding structurally and functionally adaptable, bioactive-biocatalytic self-assemblies. The platform conferred exceptional stability: enzymes withstood 20 cycles at 50 °C and retained 47.7% activity after one-year ambient storage. The assemblies accommodated diverse enzymes (ALP, GOx, HRP, SOD, CAT), adhered universally to solid surfaces, MOFs, and liquid metal microspheres, and were programmable into coatings, films, or hydrogels. Rational enzyme selection enabled biomimetic mineralization (ALP), antioxidation (SOD/CAT), and antibacterial activity (GOx). Spatial organization of cascade enzymes in core-shell nanoparticles enabled gated catalysis, while segregation on conductive supports facilitated enzyme-mediated electrochemical corrosion control. Moreover, these biointerfacing assemblies elicited favorable cell adhesion, biocompatibility, and anti-inflammatory/-infective effects
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