Bioadhesive materials capable of operating under aqueous conditions are of considerable interest for biomedical and materials science applications. Peptide-based systems represent an attractive platform for such materials due to their structural tunability, inherent biocompatibility, and ability to form supramolecular networks through noncovalent interactions. In this work, a focused library of tyrosine-containing dehydropeptides was designed and synthesized to investigate how molecular architectures influence self-assembly, hydrogel formation and adhesive properties. The peptides were synthesized using a solution-phase Boc strategy and systematically varied with respect to N-terminal protection and C-terminal functionality. The N-protected dehydropeptides formed supramolecular hydrogels through multiple gelation triggers, including pH reduction and heating–cooling cycles. Rheological characterization confirmed the formation of viscoelastic networks with tunable mechanical properties, with storage moduli reaching tens of kilopascals depending on peptide structure. Scanning electron microscopy revealed dense fibrous nanostructures consistent with supramolecular hydrogel formation. The N,C-deprotected dehydropeptides displayed reduced gelation propensity but formed cohesive films with measurable adhesive performance toward hydrophilic substrates. Lap-shear tests demonstrated high shear strengths for the hydrophilic films, highlighting their structural robustness under stress. Overall, this study provides insights into the structure–property relationships governing tyrosine-containing dehydropeptide assemblies and demonstrates their potential as minimalistic building blocks for supramolecular adhesive materials.
Pereira et al. (Thu,) studied this question.