Amyloid Structure: Conformational Diversity and Consequences
The primary structural characteristic of amyloid fibers is a predominantly β-sheet structure. These β-sheets, however, can come in two major forms: parallel and antiparallel (Figure 1a). The parallel β-sheet has another important designation, which …
Amyloid beta: structure, biology and structure-based therapeutic ...
In this paper, we review the structures, biological functions, and neurotoxicity role of Aβ. We also discuss the potential receptors that interact with Aβ and mediate Aβ intake, clearance, and metabolism. Additionally, we summarize the therapeutic developments and recent advances of different strategies for treating Alzheimer's disease.
The role of α-sheet structure in amyloidogenesis: characterization …
2022年11月23日 · De novo α-sheet peptides bind specifically to α-sheet oligomers of a variety of amyloid systems, including both bacterial and mammalian peptides and proteins. This conserved structure reveals a strategy through which to combat amyloid-associated diseases as well as to design diagnostics that can be used to identify a myriad of amyloid ...
Amyloid beta: structure, biology and structure-based …
2017年7月17日 · In this paper, we review the structures, biological functions, and neurotoxicity role of Aβ. We also discuss the potential receptors that interact with Aβ and mediate Aβ intake, clearance, and...
The Role of α-sheet in Amyloid Oligomer Aggregation and Toxicity
2018年9月21日 · De novo monomeric α-sheet peptides designed to be complementary to the structure observed in simulations inhibit amyloid aggregation and toxicity and specifically bind to the toxic oligomeric species in a variety of unrelated mammalian and bacterial amyloid systems associated with a range of diseases.
α-Sheet secondary structure in amyloid β-peptide drives ... - PNAS
2019年4月19日 · We showed that the α-sheet structure is recognized by the A11 amyloid-oligomer–specific antibody, that α-sheet peptides inhibited Aβ aggregation and blocked toxicity, and that α-sheet peptides bound specifically to oligomeric preparations of Aβ.
The Three-Dimensional Structures of Amyloids - PMC
Amyloids are highly ordered protein aggregates that are associated with both disease (including PrP prion, Alzheimer’s, and Parkinson’s) and biological function. The amyloid structure is composed of the cross-β-sheet entity, which is an almost indefinitely repeating two-layered intermolecular β-sheet motif.
Amyloid β-sheet mimics that antagonize protein aggregation …
2012年9月9日 · Here, we introduce a family of robust β-sheet macrocycles that can serve as a platform to display a variety of heptapeptide sequences from different amyloid proteins. We have tailored these...
The activities of amyloids from a structural perspective | Nature
2016年11月9日 · Amyloids are composed of pairs of tightly interacting, many stranded and repetitive intermolecular β-sheets, which form the cross-β-sheet structure. This structure enables amyloids to...
Biology of Amyloid: Structure, Function, and Regulation - Cell Press
Amyloids are highly ordered cross-β sheet protein aggregates associated with many diseases including Alzheimer's disease, but also with biological functions such as hormone storage. The cross-β sheet entity comprising an indefinitely repeating intermolecular β sheet motif is unique among protein folds.