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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 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-? spine.

SUBMITTER: Yuan D

PROVIDER: S-EPMC4845953 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature

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

Yuan Dan D Shi Junfeng J Du Xuewen X Huang Yibing Y Gao Yuan Y Xu Bing B

Journal of materials chemistry. B 20160111 7

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-<b>1P</b>) is able to a ...[more]

PMID: 27134750

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