Collagen Pentablock Copolymers Form Smectic Liquid Crystals as Precursors for Mussel Byssus Fabrication

Protein-based biological materials are important role models for the design and fabrication of next generation advanced polymers. Marine mussels (Mytilus spp.) fabricate hierarchically structured collagenous fibers known as byssal threads via bottom-up supramolecular assembly fluid protein precursors. The high degree structural organization in is intimately linked to their exceptional toughness self-healing capacity. Here, we investigated hypothesis that multidomain collagen precursor proteins, preCols, stored secretory vesicles a colloidal liquid crystal (LC) phase prior thread self-assembly. Using electron microscopy methods, including scanning TEM FIB-SEM, visualized detailed smectic preCol LC nanostructure 3D, various defects, confirming this providing quantitative insights into mesophase structure. In light these findings, performed an in-depth comparative analysis sequences from multiple Mytilid species revealing arises evolutionarily conserved ABCBA pentablock copolymer-like primary structure based on demarcations hydropathy charge distribution well terminal pH-responsive domains trigger fiber formation. These distilled principles provide inspiration strategies sustainable nanostructured polymeric potential applications engineering biomedical applications.