Illustrating the amyloid web encircling humans

Abstract

Background

The human proteome contains thousands of different proteins. A generic feature of proteins is their propensity to aggregate and form amyloid fibrils under specific conditions. Amyloids are known as paradoxical for their roles in both pathological disorders and physiological functions. State-of-the-art detection techniques have revealed that more than 50 human proteins can intrinsically form amyloid under physiological or pathological conditions.

Scope

Besides being formed endogenously, humans can be exposed to amyloids through diet, infection, and amyloid-derived materials. It has been observed in the last decade that food proteins and, materials designed from proteins contain amyloids or amyloid precursors. Humans therefore, are surrounded by an unrecognized amyloid web.

Key findings and conclusions

In light of the fact that a timely diagnosis of pathological amyloidosis is crucial for a better prognosis, this commentary puts the need to investigate the amyloid network and its potential adversities. Moreover, given that amyloids are known to cross-seed and sequester related as well as unrelated proteins, this commentary lays the groundwork for a careful examination of the proteins circulating through human systems and suggests a primer approach to construct a stratagem.