Ubiquitous Amyloids

Abstract

The common view of amyloids and prion proteins is that they are associated with many currently incurable diseases and present a great danger to an organism. This danger comes from the fact that not only prion proteins, but also the infectious form(s) of amyloids, as it has been shown recently, are able to transmit the disease. On the other hand, organisms take advantage of the strength and durability of specific forms of amyloids. Such forms do not spread any disease. Also, in nanotechnology there is a constantly growing need to employ amyloid fibrils in many industrial applications. With increasing knowledge about amyloids and prion proteins we are aware that the amyloidal state is inherent to any protein, making the problem of amyloid formation a central one in aging-related diseases. However, the “good” amyloids can be beneficial and even necessary for our health. Furthermore, because of their mechanical properties, the amyloids are of great interest to engineers.

Microglia contributes to plaque growth by cell death due to uptake of amyloid β in the brain of Alzheimer's disease mouse model

“…These aggregations are concentration dependent (Harper and Lansbury, 1997) and physiological environments are important in influencing the progression of aggregation. Moreover, Ab seeds are rarely decomposed into their soluble form once they are developed because of their stability (Greenwald and Riek, 2010;Pulawski et al, 2012;Smith et al, 2006). Moreover, Ab seeds are rarely decomposed into their soluble form once they are developed because of their stability (Greenwald and Riek, 2010;Pulawski et al, 2012;Smith et al, 2006).…”

“…Acidic conditions (pH 5-6) inside of the lysosome, a cellular organelle involved in degradation of redundant molecules, create aggregation prone environment (Hu et al, 2009;Wood et al, 1996). Moreover, Ab seeds are rarely decomposed into their soluble form once they are developed because of their stability (Greenwald and Riek, 2010;Pulawski et al, 2012;Smith et al, 2006). Ab seeds have resistance to proteinase K (PK) (Langer et al, 2011) and formaldehyde (Fritschi et al, 2014a), which can inactivate most proteins.…”

Electrochemically Induced Formation of Cytochrome c Oligomers at Soft Interfaces

“…This approach allowed the discrimination of various Aβ42 states, as Tyr10 is hidden in aggregate states . As amyloids are known to form in extracellular space and destabilise the cell membrane, the liquid−liquid interface may provide an experimental model for the investigation of oligomer and fibril formation. The interface between two immiscible electrolyte solutions (ITIES) provides a platform for the investigation into the behaviour of macromolecules based on ion transfer across the interface .…”

Small-molecule PET Tracers for Imaging Proteinopathies

“…Amyloids comprise a group of proteins of varying cellular origin, size, concentration, and function, and they are characterized by their propensity to self-aggregate into oligomeric species that progressively form fibrillar beta-pleated sheet structures (14) (Figure 2). These extended beta-sheet structures are the distinguishing feature of amyloids (15). “Amyloid” derives from the Greek “ámulon” meaning starch and was first used by the German botanist Matthias Schleiden to describe starch-like plant extracts that he identified using a crude staining method employing iodine and sulphuric acid (16).…”