“What Doesn’t Kill You Makes You Stronger”: Future Applications of Amyloid Aggregates in Biomedicine

Abstract

Amyloid proteins are linked to the pathogenesis of several diseases including Alzheimer’s disease, but at the same time a range of functional amyloids are physiologically important in humans. Although the disease pathogenies have been associated with protein aggregation, the mechanisms and factors that lead to protein aggregation are not completely understood. Paradoxically, unique characteristics of amyloids provide new opportunities for engineering innovative materials with biomedical applications. In this review, we discuss not only outstanding advances in biomedical applications of amyloid peptides, but also the mechanism of amyloid aggregation, factors affecting the process, and core sequences driving the aggregation. We aim with this review to provide a useful manual for those who engineer amyloids for innovative medicine solutions.

Solid-state packing dictates the unexpected solubility of aromatic peptides

“… 4 Many major degenerative disorders share the common etiology of aggregation into amyloid fibrils by proteins and peptides. 5 Although, in more recent times, these nanostructures have found interesting applications as advanced materials for innovative medicine solutions, tissue engineering, renewable energy, environmental science, nanotechnology, and materials science, 6 , 7 the high propensity to assemble into insoluble aggregates is very common but poses a serious limitation to the production and use of many peptides in a wide range of biotechnological and pharmaceutical applications. 1 , 8 Increasing the aqueous solubility of poorly water-soluble drugs is the most frequent requirement in the pharmaceutical analysis and formulation fields.…”

The Etiology and Pathophysiology Genesis of Benign Prostatic Hyperplasia and Prostate Cancer: A New Perspective

“…The incidental findings of prostatic amyloid transthyretin refers to cardiac amyloidosis [104], as opposed to the serum amyloid A [101][102][103]. Amyloidosis results from the accumulation of pathogenic amyloid, most of which are aggregates of misfolded proteins in a variety of tissues, which interferes with their normal physiology and function in chronic inflammatory diseases [103,[105][106][107][108][109][110]. It forms the amyloid senescence cascade hypothesis and is harmful to the non-senescent surrounding cells [111].…”

Multi-length scale structural investigation of lysozyme self-assembly

“…A deeper understanding of how nature synthesizes functional amyloids sheds light on the conditions in which pathological amyloids form. Additionally, amyloid structures can also be artificially synthetized in vitro and applied for designing novel functional materials with promising applications ( Rajagopal and Schneider, 2004 ; Hanczyc et al., 2013 ; Mains et al., 2013 ; Bolisetty and Mezzenga, 2016 ; Chaves et al., 2016 ; Knowles and Mezzenga, 2016 ; Abdelrahman et al., 2020 ). Owing to the breadth of fields that seek an accurate definition of amyloid structures, pursuing fundamental and systematic studies on the proteins’ hierarchical self-assembly mechanisms is of paramount importance.…”