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Based on the self-assembly capability of the core segment (GNNQQNY) of yeast prion Sup35, we design and synthesis a series of structurally related precursors for 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 amyloid segment into a cytotoxic precursor (N'ffyp: D- 1P ) is able to abrogate the cytotoxicity of the precursor, making the resulting peptide to be cell compatible. This work contributes a new insight to the use of enzyme to form cell compatible hydrogels of peptides cross-β spine.

The enzyme-instructed assembly of the core of yeast prion Sup35 to form supramolecular hydrogels