Yuan D.,415 South Street MS 015 |
Shi J.,415 South Street MS 015 |
Du X.,415 South Street MS 015 |
Huang Y.,415 South Street MS 015 |
And 3 more authors.
Journal of Materials Chemistry B | Year: 2016
Based on the self-assembly capability of the core segment (GNNQQNY) of yeast prion Sup35, we design and synthesise a series of structurally related precursors for the enzymatic formation of hydrogels. We found that, with the catalysis of alkaline phosphatase, the precursor becomes a hydrogelator that self-assembles in water to form nanofibers with an average width less than ten nanometers. Interestingly, the introduction of an amyloid segment into a cytotoxic precursor (N′ffyp: d-1P) is able to abrogate the cytotoxicity of the precursor, making the resulting peptide cell compatible. This work contributes a new insight into the use of enzymes to form cell compatible hydrogels of peptide cross-β spine. © The Royal Society of Chemistry 2016. Source