Work

Bioinspired Bromination Enables Extensible, Strain‐Stiffening Resilin Peptide Scaffolds with Tunable Degradation

Year: 2025

Type: article

Abstract: Short, bio‐inspired peptides hold promise for creating functional materials with unique structural and biochemical properties, yet their generally limited tunability of mechanical properties often restricts their utility. Inspired by Nature's strategic use of halogenation to strengthen biomaterials, here, a novel electrospun scaffold is reported in which a brominated resilin‐derived peptide SDSY(3,5Br)GAP (BR peptide), endowed with self‐assembling properties, serves as the principal building block, supported by a gelatin matrix. The BR peptide transitions to β‐turn‐rich assemblies upon electrospinning, resulting in the hybrid scaffolds with a twofold increase in modulus beyond ≈50% strain and good recovery properties, thereby mimicking the strain‐stiffening behaviour of natural elastomers. Notably, such features are completely absent in the nonbrominated peptide (WR peptide) scaffolds, emphasizing the crucial structural role given by bromine atoms. Additionally, BR peptide‐based systems exhibited superior proteolytic stability and notable antioxidant activity together with proven noncytotoxic effects, underscoring their potential for applications spacing from soft tissue engineering to adaptive textiles and wearable soft actuators. Collectively, this unique combination of mechanical resilience, proteolytic stability, antioxidant functionality, and biocompatibility highlights halogenation as an effective strategy for tuning the performance of peptide‐based materials, ultimately bridging the gap between synthetic polymers and Nature's most resilient protein materials.

Source: Advanced Functional Materials

DOI: 10.1002/adfm.202518804