Catechol-functionalized proteins in mussel holdfasts are essential for underwater adhesion and cohesion and have inspired countless synthetic polymeric materials and devices. However, as catechols are prone to oxidation, long-term performance and stability of these inventions awaits effective antioxidation strategies. In mussels, catechol-mediated interactions are stabilized by 'built-in' homeostatic redox reservoirs that restore catechols oxidized to quinones. Mussel byssus has a typical 'core-shell' architecture in which the core is a degradable fibrous block copolymer consisting of collagen and fibroin coated by robust protein networks stabilized by bis-catecholato-metal and tris-catecholato-metal ion complexes. The coating is well-adapted to protect the core against abrasion, hydrolysis and microbial attack, but it is not impervious to oxidative damage, which, during function, is promptly repaired by redox poise via coacervated catechol-rich and thiol-rich reducing interlayers and inclusions. However, when the e