Current therapies for Alzheimer's disease (AD) can provide a moderate symptomatic reduction or delay progression at various stages of the disease, but such treatments ultimately do not arrest the advancement of AD. As such, novel approaches for AD treatment and prevention are urgently needed. We here provide both experimental and computational evidence that pristine graphene and graphene-oxide ...

Inhibition of amyloid fibril formation could benefit patients with systemic amyloidosis. In this group diseases, deposition fibrils derived from normally soluble proteins leads to progressive tissue damage and organ failure. Amyloid is a complex process, where several individual steps be targeted. Several small molecules have been proposed as inhibitors formation. However, the exact mechanism a...

Using tip-enhanced Raman spectroscopy (TERS) imaging with a lateral optical resolution of ~16 nm, the heterogeneity A?(1-42) fibrils implicated in Alzheimer’s disease is investigated. The amount and spatial distribution TERS bands assigned to aromatic amino acid residues (histidine, tyrosine phenylalanine) parallel ?-sheet random coil secondary structures suggest that both surface core are prob...

The unique enhanced sensitivity of vibrational circular dichroism (VCD) to the formation and development of amyloid fibrils in solution is extended to four additional fibril-forming proteins or peptides where it is shown that the sign of the fibril VCD pattern correlates with the sense of supramolecular filament chirality and, without exception, to the dominant fibril morphology as observed in ...

Aggregation of Ig light chains to form amyloid fibrils is a characteristic feature of light-chain amyloidosis, a light-chain deposition disease. A recombinant variable domain of the light chain SMA was used to form amyloid fibrils in vitro. Fibril formation was monitored by atomic force microscopy imaging. Single filaments 2.4 nm in diameter were predominant at early times; protofibrils 4.0 nm ...

Amyloid aggregation is a hallmark of several degenerative diseases affecting the brain or peripheral tissues, whose intermediates (oligomers, protofibrils) and final mature fibrils display different toxicity. Consequently, compounds counteracting amyloid aggregation have been investigated for their ability (i) to stabilize toxic amyloid precursors; (ii) to prevent the growth of toxic oligomers ...

The expanding universe of amyloid has revealed an intriguing new galaxy, invasive candidiasis, with the publication by Gilchrist et al in this issue of the Journal. Invasive infection of the gut by Candida albicans is a serious, intractable condition that occurs most commonly but not exclusively in neutropenic patients and for which there is very poorly effective treatment. Gilchrist et al now ...

Despite its importance in biological phenomena, a comprehensive understanding of the mechanism of amyloid formation remains elusive. Here, we use atomic force microscopy to map the formation of beta2-microglobulin amyloid fibrils with distinct morphologies and persistence lengths, when protein concentration, pH and ionic strength are varied. Using the resulting state-diagrams, we demonstrate th...

Various proteins and peptides are able to self assemble into amyloid fibrils that are associated with disease. Structural characterisation of these fibres is limited by their insoluble and heterogeneous nature. However, advances in various techniques including X-ray diffraction, cryo-electron microscopy and solid state NMR have provided detailed information on various amyloid fibrils, from the ...

Amyloid fibrils are assemblies of misfolded proteins and are associated with pathological conditions such as Alzheimer's disease and the spongiform encephalopathies. In the amyloid diseases, a diverse group of normally soluble proteins self-assemble to form insoluble fibrils. X-ray fibre diffraction studies have shown that the protofilament cores of fibrils formed from the various proteins all ...