UV-light exposed prion protein fails to form amyloid fibrils. [PDF]
PLoS ONE, 2008 Amyloid fibril formation involves three steps; structural perturbation, nucleation and elongation. We have investigated amyloidogenesis using prion protein as a model system and UV-light as a structural perturbant.
Abhay Kumar Thakur, Ch Mohan Rao
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Effect of pH on the Formation, Disintegration and Antioxidant Activity of Mung Bean Protein Fibrils [PDF]
AntioxidantsProtein fibrils are highly ordered structures. Mung bean protein (MBP) fibrils were fabricated after heating under acidic condition. The formation mechanism, structural variety and antioxidant capacities of mung bean protein fibrils were investigated ...
Yike Tian +4 more
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The effects of whey protein fibrils on the linear and non-linear rheological properties of a gluten-free dough [PDF]
Frontiers in Nutrition, 2022 The increasing awareness of the celiac disease, an autoimmune disorder caused by the consumption of products containing gluten, has led to a growing interest in the development of gluten-free bakery products.
Shengyue Shan +6 more
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Morphological and Biophysical Study of S100A9 Protein Fibrils by Atomic Force Microscopy Imaging and Nanomechanical Analysis [PDF]
BiomoleculesAtomic force microscopy (AFM) imaging enables the visualization of protein molecules with high resolution, providing insights into their shape, size, and surface topography.
Ana P. Carapeto +3 more
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Secondary Nucleation and the Conservation of Structural Characteristics of Amyloid Fibril Strains
Frontiers in Molecular Biosciences, 2021 Amyloid fibrils are ordered protein aggregates and a hallmark of many severe neurodegenerative diseases. Amyloid fibrils form through primary nucleation from monomeric protein, grow through monomer addition and proliferate through fragmentation or ...
Saeid Hadi Alijanvand +2 more
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AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
Nature Communications, 2021 Systemic AA amyloidosis is a protein misfolding disease caused by the formation of amyloid fibrils from serum amyloid A (SAA) protein. Here, the authors present the cryo-EM structures of AA amyloid fibrils isolated from mouse tissue and in vitro formed ...
Akanksha Bansal +8 more
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Protein-based luminescent aerogels with elastic properties
Green Chemistry Letters and Reviews, 2022 Gelatin is a famous gel-forming proteinaceous material with excellent hydrogelation properties. Herein, we report that protein nanofibrils (PNFs) can be employed to form hybrids with gelatin that can be converted to aerogels with attractive mechanical ...
Yusheng Yuan, Niclas Solin
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Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq
Antibiotics, 2021 Hfq is a bacterial regulator with key roles in gene expression. The protein notably regulates translation efficiency and RNA decay in Gram-negative bacteria, thanks to its binding to small regulatory noncoding RNAs. This property is of primary importance
Florian Turbant +6 more
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Surface Properties of Aqueous Dispersions of Bovine Serum Albumin Fibrils
Colloids and Interfaces, 2023 The surface properties of aqueous dispersions of worm-like fibril aggregates of bovine serum albumin (BSA) differ from those of the adsorption layers of the native protein. The dispersions of BSA fibrils are characterized by slower changes of the surface
Alexander Akentiev +4 more
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Cryo-EM demonstrates the in vitro proliferation of an ex vivo amyloid fibril morphology by seeding
Nature Communications, 2022 Here, the authors present the cryo-EM structure of in vitro amyloid fibrils from recombinant SAA1.1 protein that were formed by seeding with fibrils purified from systemic AA amyloidosis tissue.
Thomas Heerde +12 more
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