Peptide Amyloid Surface Display | Zendy

Marisa A. Rubio | Zendy; Diana E. Schlamadinger | Zendy; Ellen M. White | Zendy; Andrew D. Miranker | Zendy

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Peptide Amyloid Surface Display

Author(s) -

Marisa A. Rubio,

Diana E. Schlamadinger,

Ellen M. White,

Andrew D. Miranker

Publication year - 2014

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.43

H-Index - 253

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/bi5011442

Subject(s) - homomeric , amyloid (mycology) , islet , chemistry , peptide , biophysics , fiber , amyloid fibril , sequence (biology) , insulin , function (biology) , biochemistry , microbiology and biotechnology , amyloid β , biology , endocrinology , medicine , inorganic chemistry , disease , organic chemistry , protein subunit , gene

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 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.

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