Abstract
Bionanomaterials have great potential for applications in tissue engineering and regenerative medicine. Recently, amyloid-like fibrils have been used in bionanomaterials preparation due to their stability and biocompatibility. Covalent dityrosine bond formation has been identified as a useful tool in the design of such bionanomaterials. In this study, two short amyloidogenic peptides containing tyrosine residues with the amino acid sequence HYFNIF and VIYKI, were used as a model system to investigate the effect of oxidation and their ability to form dityrosine cross-links. Using a range of biophysical techniques, we showed that both HYFNIF and VIYKI form dityrosine cross-linked fibrils using copper-catalysis, and phosphate buffer is more efficient in dityrosine formation. Dityrosine forms more rapidly in VIYKI fibrils compared to HYFNIF due to the fibrillar architecture. Dityrosine cross-linked HYFNIF and VIYKI fibrils could be useful to prepare bionanomaterials.
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