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Issue 25, 2018
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Total chemical synthesis and biophysical properties of a designed soluble 24 kDa amyloid analogue

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Abstract

Discovering molecular probes that specifically recognize distinct amyloid structures is highly important for physiological studies of protein-misfolding diseases as well as for the development of diagnostic reagents and inhibitors of amyloid self-assembly. Here, we demonstrate an approach that allows for identification of N-methylated peptides that are specific binders for a particular amyloid fiber subtype (or polymorph). Protein design and chemical synthesis were used to produce covalently tethered amyloid analogues with molecular masses approaching 24 kDa and containing nine copies of an amyloidogenic peptide. Such engineered constructs served as a molecular testing platform to evaluate the aggregation properties and solubility as a function of N-methylation pattern. An advantage of the method is the possibility of biophysical characterization of amyloid constructs in solution.

Graphical abstract: Total chemical synthesis and biophysical properties of a designed soluble 24 kDa amyloid analogue

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Publication details

The article was received on 19 Apr 2018, accepted on 24 May 2018 and first published on 25 May 2018


Article type: Edge Article
DOI: 10.1039/C8SC01790E
Citation: Chem. Sci., 2018,9, 5594-5599
  • Open access: Creative Commons BY license
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    Total chemical synthesis and biophysical properties of a designed soluble 24 kDa amyloid analogue

    R. Boehringer, B. Kieffer and V. Torbeev, Chem. Sci., 2018, 9, 5594
    DOI: 10.1039/C8SC01790E

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