Photocurable Polypeptide and Recombinant-Protein Materials: Sequence, Functionalisation, Folding and Network Attribution

Abstract

Photocurable recombinant proteins and engineered polypeptides offer sequence-level control that is unavailable in most natural extracts or synthetic polymers. That control is meaningful only if molecular identity, folding state, functionalisation and network formation remain traceable through processing. Chemical modification can introduce photocurable groups but may also alter charge, secondary structure or bioactive motifs. Conversely, recombinant sequence design can place reactive residues or domains at defined positions and create proteins that self-assemble before or after light exposure. This review develops a qualification framework that separates sequence identity, molecular assembly, chemical functionalisation and photochemical crosslinking. Recombinant collagen and methacrylated tropoelastin are used as representative examples, but the focus is mechanism rather than one protein family. The key question is network attribution: which observed mechanical or biological property comes from the encoded protein sequence, which from higher-order assembly and which from the light-created covalent network? ER-327 · Version 0.5.