Issue 7, 2016

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.

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

Supplementary files

Article information

Article type
Paper
Submitted
09 Nov 2015
Accepted
08 Jan 2016
First published
11 Jan 2016

J. Mater. Chem. B, 2016,4, 1318-1323

Author version available

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

D. Yuan, J. Shi, X. Du, Y. Huang, Y. Gao, A. A. Baoum and B. Xu, J. Mater. Chem. B, 2016, 4, 1318 DOI: 10.1039/C5TB02346G

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