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Issue 17, 2017, Issue in Progress
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Sucrose modulates insulin amyloid-like fibril formation: effect on the aggregation mechanism and fibril morphology

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Abstract

Co-solutes, such as sugars, are used in in vitro protein aggregation experiments to mimic crowding and, in general, complex environments. Sugars often increase the stability of the native protein structure by affecting inter- and intramolecular protein–protein interactions. This, in turn, modifies the protein self-assembly pathways. Using a combination of fluorescence spectroscopy, synchrotron radiation circular dichroism and transmission electron microscopy, we study the kinetics of formation and structural properties of human insulin fibrils in the presence of sucrose. The presence of sucrose results in a delay of the onset of fibrillation. Moreover, it leads to a dramatic change in both the morphology and overall amount of fibrils. Our results emphasize that the detailed composition of protein surroundings likely influences not only the fibrillation kinetics but also the balance between different species, potentially determining fibril strains with different biological activities. This aspect is crucial in the etiology of pathologies associated with amyloidosis.

Graphical abstract: Sucrose modulates insulin amyloid-like fibril formation: effect on the aggregation mechanism and fibril morphology

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Publication details

The article was received on 26 Oct 2016, accepted on 29 Jan 2017 and first published on 07 Feb 2017


Article type: Paper
DOI: 10.1039/C6RA25872G
Citation: RSC Adv., 2017,7, 10487-10493
  • Open access: Creative Commons BY-NC license
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    Sucrose modulates insulin amyloid-like fibril formation: effect on the aggregation mechanism and fibril morphology

    C. Marasini, V. Foderà and B. Vestergaard, RSC Adv., 2017, 7, 10487
    DOI: 10.1039/C6RA25872G

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