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Amyloid Oligomers, Protofibrils and Fibrils

2019
Amyloid diseases are of major concern all over the world due to a number of factors including: (i) aging population, (ii) increasing life span and (iii) lack of effective pharmacotherapy options. The past decade has seen intense research in discovering disease-modifying multi-targeting small molecules as therapeutic options.
Mohammad Khursheed, Siddiqi   +4 more
openaire   +2 more sources

Mesoscopic Properties of Semiflexible Amyloid Fibrils

Langmuir, 2004
We have determined the contour length, persistence length, bending rigidity, and critical percolation concentration for semiflexible amyloid fibrils formed from the globular proteins beta-lactoglobulin, bovine serum albumin, and ovalbumin. The persistence length was estimated using an adjusted random contact model for highly charged semiflexible chains.
Sagis, L.M.C.   +2 more
openaire   +3 more sources

Inhibitors of amyloid fibril formation

Many diseases are caused by misfolded and denatured proteins, leading to neurodegenerative diseases. In recent decades researchers have developed a variety of compounds, including polymeric inhibitors and natural compounds, antibodies, and chaperones, to inhibit protein aggregation, decrease the toxic effects of amyloid fibrils, and facilitate ...
Elaheh, Tavili   +2 more
openaire   +2 more sources

Biotechnological applications of amyloid fibrils

Protein aggregates and amyloid fibrils have special qualities and are used in a variety of biotechnological applications. They are extensively employed in bioremediation, biomaterials, and biocatalysis. Because of their capacity to encapsulate and release pharmaceuticals and their sensitivity to certain molecules, respectively, they are also used in ...
Mohsen, Nabi Afjadi   +3 more
openaire   +2 more sources

Amyloid Neuropathy: Relationship between Amyloid Fibrils and Macrophages

Ultrastructural Pathology, 1984
A case of amyloid neuropathy associated with a multiple myeloma IgG light chain is reported. Under light microscopy the peripheral nerve exhibited several amyloid deposits. Electron microscopy revealed numerous amyloid deposits; at their periphery, macrophagic histiocytes were observed, containing a few tufts of parallel fibrils in their cytoplasm.
A, Vital, C, Vital
openaire   +2 more sources

Self-Assembly of Ovalbumin into Amyloid and Non-Amyloid Fibrils

Biomacromolecules, 2012
We study the fibrillation pathway of ovalbumin protein and report the simultaneous formation of several types of fibrils, with clear structural and physical differences. We compare the fibrillation mechanisms at low pH with and without salt, and follow the kinetics of fibrils growth by atomic force microscopy (AFM), static and dynamic light scattering (
Lara C   +4 more
openaire   +3 more sources

Amyloid Fibrils in Bionanotechnology

Australian Journal of Chemistry, 2004
An amyloid fibril is a highly ordered, insoluble form of protein that results when a normally soluble protein aggregates via a self-association process to form a structured nanotube. Such fibrils can now be routinely generated from purified proteins in the laboratory, and have attracted burgeoning interest due to their role in a variety of disease ...
Sarah H. Waterhouse, Juliet A. Gerrard
openaire   +1 more source

Structural Evolution of Fibril Polymorphs During Amyloid Assembly

Cell, 2023
Martin Wilkinson   +2 more
exaly  

Amyloid Fibrils Aerogel for Sustainable Removal of Organic Contaminants From Water

Advanced Materials, 2020
Laura Nyström   +2 more
exaly  

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