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Nevertheless, collagen assembly in vitro to create ideal artificial corneal substitutes with human cornea comparable thickness and optics is still limited. Here, glycerol as a regulator can reconcile collagen thickness, transparency, and permeability, a conflicting goal by current keratoprosthesis strategies. Structure analysis reveals that glycerol treatment induces collagen hydrogels to undergo a sequential three\u2010step multiscale structural evolution: weakened collagen crystallization at the molecular level, followed by ordered and distanced microfibril packaging at the nanoscale, and ultimately lamellar structure as well as fibril diameter and spacing\u2010dependent optics at a macroscopic level. Such ultrastructure is then stabilized by oxazolidine crosslinking to obtain a collagen\u2010based artificial corneal substitute (Col\u2010Gly\u2010OX) with optimal integration of optical clarity, mechanical robustness, high permeability, manufacturability, easy preservation and in vitro biocompatibility. Further in vivo study demonstrates that Col\u2010Gly\u2010OX displays excellent tissue integration, epithelialization, and stromal remodeling in a rabbit lamellar keratectomy. 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