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

Abstract

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.