Amyloid - Wikipedia
Amyloids are aggregates of proteins characterised by a fibrillar morphology of typically 7–13 nm in diameter, a β-sheet secondary structure (known as cross-β) and ability to be stained by particular dyes, such as Congo red. [1] . In the human body, amyloids have been linked to the development of various diseases. [2] .
Amyloid fibrils: Abnormal protein assembly - PMC - PubMed …
Amyloid fibrils are extremely strong, highly ordered and organized fibers that can be formed by a large number of proteins and peptides. Their stability and insolubility means that they are useful in a large number of naturally occurring forms as well as bionanotechnology.
Amyloid Fibril - an overview | ScienceDirect Topics
Amyloid fibrils are non-native protein structures that demonstrate a host of desirable properties, making these fibers attractive components for nanotechnology and biomedicine (Gras, 2007; Hamada et al., 2004; Macphee and Woolfson, 2004; …
Current Understanding of the Structure, Stability and Dynamic ...
Amyloid fibrils are supramolecular protein assemblies represented by a cross-β structure and fibrous morphology, whose structural architecture has been previously investigated. While amyloid fibrils are basically a main-chain-dominated structure ...
Structural evolution of fibril polymorphs during amyloid assembly
2023年12月21日 · Here, we used cryo-EM to determine structures of amyloid fibrils at different times during in vitro fibrillation of a disease-related variant of human islet amyloid polypeptide (IAPP-S20G). Strikingly, the fibrils formed in the lag, growth, and plateau phases have different structures, with new forms appearing and others disappearing as ...
Amyloid formation as a protein phase transition - Nature
2023年6月27日 · The formation of amyloid fibrils is a general class of protein self-assembly behaviour, which is associated with both functional biology and the development of a number of disorders, such as...
The Expanding Amyloid Family: Structure, Stability, Function, and ...
Unlike globular proteins, amyloid proteins flatten and stack into unbranched fibrils. Stranger still, a single protein sequence can adopt wildly different two-dimensional conformations, yielding distinct fibril polymorphs. Hence, an amyloid protein may define distinct diseases depending on its …
A new era for understanding amyloid structures and disease
2018年9月20日 · We discuss how amyloid structure may affect the ability of fibrils to spread to different sites in the cell and between organisms in a prion-like manner, along with their roles in disease....
Molecular rules governing the structural polymorphism of amyloid ...
2023年11月2日 · Amyloid fibrils are hallmarks of various neurodegenerative diseases. The structural polymorphism of amyloid fibrils holds significant pathological importance in diseases. This review aims to provide an in-depth overview on the complexity of amyloid fibrils’ structural polymorphism and its implications in disease pathogenesis.
Amyloid fibrils: abnormal protein assembly - PubMed
In this chapter we will highlight the key scientific findings and discuss how the stability of amyloid fibrils impacts on bionanotechnology. 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.