Enzymatic assembly of adhesive molecular networks with sequence-dependent mechanical properties inspired by mussel foot proteins

By inserting short peptide motifs derived from Mfp-3 and Mfp-5 into elastin-like polypeptides (ELPs), we created several recombinant protein polymers that can form adhesive hydrogels upon enzymatic oxidation. The resulting materials exhibited sequence-dependent bulk mechanical properties and strong adhesiveness. The materials also showed excellent cytocompatibility toward encapsulated human alveolar epithelial cells. This study illustrates a new strategy for designing adhesive materials for biomedical and research purposes.