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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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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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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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Prion, 2008 Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in organs and tissues. Amyloid is insoluble and is structurally dominated by beta-sheet structure. Unlike other fibrous proteins it does not commonly have a structural, supportive or motility role but is associated with the pathology seen in a range of diseases known as
Roma N, Rambaran, Louise C, Serpell
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Protein Fibrillation under Crowded Conditions
Biomolecules, 2022 Protein amyloid fibrils have widespread implications for human health. Over the last twenty years, fibrillation has been studied using a variety of crowding agents to mimic the packed interior of cells or to probe the mechanisms and pathways of the process.
Annelise H. Gorensek-Benitez +2 more
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DNA-Guided Assembly for Fibril Proteins [PDF]
Mathematics, 2021 Current advances in computational modelling and simulation have led to the inclusion of computer scientists as partners in the process of engineering of new nanomaterials and nanodevices. This trend is now, more than ever, visible in the field of deoxyribonucleic acid (DNA)-based nanotechnology, as DNA’s intrinsic principle of self-assembly has been ...
Alexandru Amărioarei +11 more
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