Alzheimer's disease is the most common form of dementia, with amyloid protein assembly associated with the pathogenesis of disease. Thus it is of utmost importance to reveal the detailed structure of the amyloid protein aggregates. In article 1500369, F. Besenbacher, M. Dong and co-workers discover a new parallel-like β-strand molecular monolayer structure of amyloid peptide at hydrophobic inte...

Insertion of an anthranilic acid in an amyloidogenic peptide sequence generates a novel conformationally restricted α/β-hybrid peptide that inhibits amyloid formation of Aβ(1-40) and disrupts preformed fibrillar aggregates in vitro. Such β-sheet breaker hybrid peptides (BSBHps) may be useful for designing novel physiologically important compounds relevant to diverse amyloidoses and for studying...

Neurovascular dysfunction is an integral part of Alzheimer disease (AD). Changes in the brain vascular system may contribute in a significant way to the onset and progression of cognitive decline and the development of a chronic neurodegenerative process associated with accumulation of amyloid β-peptide (Aβ) in brain and cerebral vessels in AD individuals and AD animal models. Here, we review t...

Amyloid-β peptide (Aβ) is still best known as a molecule to cause Alzheimer's disease (AD) through accumulation and deposition within the frontal cortex and hippocampus in the brain. Thus, strategies on developing AD drugs have been focused on the reduc-tion of Aβ in the brain. Since accumulation of Aβ depends on the rate of its synthesis and clearance, the metabolic pathway of Aβ in the brain ...

The amyloid protein aggregation associated with diseases such as Alzheimer's, Parkinson's and type II diabetes (among many others) features a bewildering variety of β-sheet-rich structures in transition from native proteins to ordered oligomers and fibres. The variation in the amino-acid sequences of the β-structures presents a challenge to developing a model system of β-sheets for the study of...

Using a simple in vitro amyloidopathy CAD neuronal model, infrared (IR) 1068 nm light treatment (5 x 3 minutes) was investigated as a novel neuroprotection strategy. Synthetic human β-amyloid(1-42) peptide was subjected to aggregation in a test-tube, and shown to form fibrils of a range of sizes (individually ~10 μm), which compromised the cellular nuclear integrity of CAD cells in culture, and...