Sucrose modulates insulin amyloid-like fibril formation: effect on the aggregation mechanism and fibril morphology
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Sucrose modulates insulin amyloid-like fibril formation: effect on the aggregation mechanism and fibril morphology. / Marasini, Carlotta; Foderà, Vito; Vestergaard, Bente.
In: RSC Advances, Vol. 7, 2017, p. 10487-10493.Research output: Contribution to journal › Journal article › peer-review
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T1 - Sucrose modulates insulin amyloid-like fibril formation: effect on the aggregation mechanism and fibril morphology
AU - Marasini, Carlotta
AU - Foderà, Vito
AU - Vestergaard, Bente
PY - 2017
Y1 - 2017
N2 - 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.
AB - 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.
U2 - 10.1039/C6RA25872G
DO - 10.1039/C6RA25872G
M3 - Journal article
VL - 7
SP - 10487
EP - 10493
JO - RSC Advances
JF - RSC Advances
SN - 2046-2069
ER -
ID: 173322867