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Issue 7, 2005
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Template-controlled conformational patterns of insulin fibrillar self-assembly reflect history of solvation of the amyloid nuclei

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Abstract

In the presence of ethanol, insulin forms amyloid morphologically distinct from the ambient specimen. Due to stability of fibrils and the autocatalytic character of the process, the two amyloid templates, when seeded, replicate the initial morphologies (and inter-β-strand hydrogen bonding patterns) regardless of the environmental biases, such as the cosolvent presence. Such “templated memory” effect is advantageous in synthesizing structurally uniform protein nanofibrils under conditions favoring alternative “wild” forms. This also appears to parallel “prion strains” phenomenon, suggesting that “strains” may reflect a generic trait in all amyloids including those not associated with disease.

Graphical abstract: Template-controlled conformational patterns of insulin fibrillar self-assembly reflect history of solvation of the amyloid nuclei

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Publication details

The article was received on 14 Feb 2005, accepted on 23 Feb 2005 and first published on 28 Feb 2005


Article type: Communication
DOI: 10.1039/B502255J
Citation: Phys. Chem. Chem. Phys., 2005,7, 1349-1351
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    Template-controlled conformational patterns of insulin fibrillar self-assembly reflect history of solvation of the amyloid nuclei

    W. Dzwolak, R. Jansen, V. Smirnovas, A. Loksztejn, S. Porowski and R. Winter, Phys. Chem. Chem. Phys., 2005, 7, 1349
    DOI: 10.1039/B502255J

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