Unfolding and Reassembling Keratin: Rebuilding a Natural Structural Protein into New Materials

Feathers, hair and wool owe their resilience to keratin. Hydrogen bonds, hydrophobic contacts and disulfide crosslinks organise its chains across several length scales into some of nature’s toughest materials. But what happens when that hierarchy is unfolded, and can the freed protein chains be reassembled into new material architectures?   This seminar first uses feather keratin as a model system to link processing, molecular organisation and material properties. Ultrasound-assisted alkaline processing at controlled temperatures shows how deconstruction and regeneration reshape keratin’s molecular-weight distribution, secondary structure, disulfide connectivity, thermal behaviour and mesoscale morphology. The key message is that extraction is not just a recovery step. Processing history sets the structure of the regenerated protein, and that structure governs how it assembles and performs. These differences appear directly in the rheological, interfacial and mechanical behaviour of keratin-based materials.   The talk closes with ongoing work here at CIC nanoGUNE within the ReWOOLVE project, which extends these questions from feather keratin to coarse wool. The focus moves from regeneration to controlled assembly: green solvent systems are combined with solution processing and electrospinning to produce regenerated keratin micro- and nanofibres. A parallel line of work explores whether peptide sequences and simplified molecular models can reveal the mechanisms behind protein association and fibre formation, and eventually serve as molecular instructions for controlling them. Rather than treating keratin waste as just a feedstock, this research asks whether a natural protein’s hierarchical design can be unfolded, understood and reassembled into new functional materials.