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monellin/amiloidosi
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Amyloid-like aggregates of a plant protein: a case of a sweet-tasting protein, monellin.
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We report here a novel case of amyloid-like aggregation of a plant protein. A sweet-tasting protein, monellin, experiences an irreversible heat denaturation at pH 2.5 and 85 degrees C. Addition of 100 mM NaCl couples this process with protein aggregation. The aggregates were structured as regular
Amyloid fibril formation by the chain B subunit of monellin occurs by a nucleation-dependent polymerization mechanism.
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Proteins possessing very different structures, or even no structure, form amyloid fibrils that are very similar in internal structure. This suggests that the mechanisms by which amyloid fibrils form might be very similar, irrespective of whether the fibrils are associated with disease or with normal
Multistep nucleus formation and a separate subunit contribution of the amyloidgenesis of heat-denatured monellin.
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Monellin (MN) is a sweet-tasting plant protein known to form fibrous aggregates in the heat-denatured state. Here the amyloid-type aggregation process of MN is extensively characterized. The amyloidgenesis was initiated in a highly denatured state of MN. A seeding effect of skipping a lag phase of
Aggregation mechanisms of cystatins: a comparative study of monellin and oryzacystatin.
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Identification of diseases caused by protein misfolding has increased interest in the way proteins adopt non-native conformations and form aggregates. In this study we address the question of how proteins sharing the same fold respond to destabilizing environmental conditions. We have studied the
Charge dependent retardation of amyloid β aggregation by hydrophilic proteins.
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The aggregation of amyloid β peptides (Aβ) into amyloid fibrils is implicated in the pathology of Alzheimer's disease. In light of the increasing number of proteins reported to retard Aβ fibril formation, we investigated the influence of small hydrophilic model proteins of different charge on Aβ
Understanding the self-assembly pathways of a single chain variant of monellin: A first step towards the design of sweet nanomaterials.
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Peptides and proteins possess an inherent tendency to self-assemble, prompting the formation of amyloid aggregates from their soluble and functional states. Amyloids are linked to many devastating diseases, but self-assembling proteins can also represent formidable tools to produce new and
The effect of nanoparticles on amyloid aggregation depends on the protein stability and intrinsic aggregation rate.
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Nanoparticles interfere with protein amyloid formation. Catalysis of the process may occur due to increased local protein concentration and nucleation on the nanoparticle surface, whereas tight binding or a large particle/protein surface area may lead to inhibition of protein aggregation. Here we
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