"Designing Peptide-Polymer Conjugates to Study Structure-Properties in Silk-Mimetic Hydrogels"
Nature is capable of making soft materials with extreme mechanical properties, such as spider
silk, whose hierarchical structure consists of crystalline domains for strength and amorphous
domains for extensibility. Attempts to genetically engineer this structure are limited by reliance
on sequences of small amino acids, such as alanine, that poorly form sheet-like (β-sheet)
structures, and by biological constraints on incorporating more hydrophobic residues, leaving the
optimal design for silk-mimetic hydrogels unclear. In this study, hydrophobic β-sheet-forming
peptides were carefully designed with aggregation-prone amino acids modified to prevent
premature aggregation, conjugated to hydrophilic polymers, and self-assembled into hydrogels.
The resulting materials exhibited striking, composition-dependent mechanical properties directly
linked to nanoscale β-sheet content and polymer morphology. This study offers valuable insights
into the rational design of next-generation stable, tunable, and reproducible silk-mimetic
biomaterials, expanding the potential of such materials for applications in tissue engineering,
wound healing, and drug delivery.