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Peptide amyloid surface display.

ABSTRACT: Homomeric self-assembly of peptides into amyloid fibers is a feature of many diseases. A central role has been suggested for the lateral fiber surface affecting gains of toxic function. To investigate this, a protein scaffold that presents a discrete, parallel ?-sheet surface for amyloid subdomains up to eight residues in length has been designed. Scaffolds that present the fiber surface of islet amyloid polypeptide (IAPP) were prepared. The designs show sequence-specific surface effects apparent in that they gain the capacity to attenuate rates of IAPP self-assembly in solution and affect IAPP-induced toxicity in insulin-secreting cells.

SUBMITTER: Rubio MA

PROVIDER: S-EPMC4318585 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature

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Peptide amyloid surface display.

Rubio Marisa A MA Schlamadinger Diana E DE White Ellen M EM Miranker Andrew D AD

Biochemistry 20150120 4

Homomeric self-assembly of peptides into amyloid fibers is a feature of many diseases. A central role has been suggested for the lateral fiber surface affecting gains of toxic function. To investigate this, a protein scaffold that presents a discrete, parallel β-sheet surface for amyloid subdomains up to eight residues in length has been designed. Scaffolds that present the fiber surface of islet amyloid polypeptide (IAPP) were prepared. The designs show sequence-specific surface effects apparen ...[more]

PMID: 25541905

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