Probing Chemical Complexity of Amyloid Plaques in Alzheimer's Disease Mice using Hyperspectral Raman Imaging.

One of the distinctive pathological features of Alzheimer's disease (AD) is the deposition of amyloid plaques within the brain of affected individuals. These plaques have traditionally been investigated using labeling techniques such as immunohistochemical imaging. However, the use of labeling can disrupt the structural integrity of the molecules being analyzed.

Regioselective Tip-Enhanced Raman Spectroscopy of Lipid Membranes with Sub-Nanometer Axial Resolution.

Noninvasive and label-free analysis of cell membranes at the nanoscale is essential to comprehend vital cellular processes. However, conventional analytical tools generally fail to meet this challenge due to the lack of required sensitivity and/or spatial resolution. Herein, we demonstrate that tip-enhanced Raman spectroscopy (TERS) is a powerful nanoanalytical tool to analyze dipalmitoylphosphatidylcholine (DPPC) bilayers and human cell membranes with submolecular resolution in the vertical direction.

Nanoscale chemical analysis of 2D molecular materials using tip-enhanced Raman spectroscopy.

Two-dimensional (2D) molecular materials have attracted immense attention due to their unique properties, promising a wide range of exciting applications. To understand the structure-property relationship of these low-dimensional materials, sensitive analytical tools capable of providing structural and chemical characterisation at the nanoscale are required. However, most conventional analytical techniques fail to meet this challenge, especially in a label-free and non-destructive manner under ambient conditions.

Nanoscale Chemical Imaging of Human Cell Membranes Using Tip-Enhanced Raman Spectroscopy.

Lack of appropriate tools for visualizing cell membrane molecules at the nanoscale in a non-invasive and label-free fashion limits our understanding of many vital cellular processes. Here, we use tip-enhanced Raman spectroscopy (TERS) to visualize the molecular distribution in pancreatic cancer cell (BxPC-3) membranes in ambient conditions without labelling, with a spatial resolution down to ca. 2.

Visualizing Surface Phase Separation in PS-PMMA Polymer Blends at the Nanoscale.

Phase-separated polymer blend films are an important class of functional materials with numerous technological applications in solar cells, catalysis, and biotechnology. These technologies are underpinned by the precise control of phase separation at the nanometer length-scales, which is highly challenging to visualize using conventional analytical tools. Herein, we introduce tip-enhanced Raman spectroscopy (TERS), in combination with atomic force microscopy (AFM), confocal Raman spectroscopy, and X-ray photoelectron spectroscopy (XPS), as a sensitive nanoanalytical method to determine lateral and vertical phase-separation in polystyrene (PS)-poly(methyl methacrylate) (PMMA) polymer blend films.

Amyloid β interaction with model cell membranes - What are the toxicity-defining properties of amyloid β?

Disruption of the neuronal membrane by toxic amyloid β oligomers is hypothesized to be the major event associated with Alzheimer's disease's neurotoxicity. Misfolding of amyloid β is followed by aggregation via different pathways in which structurally different amyloid β oligomers can be formed. The respective toxic actions of these structurally diverse oligomers can vary significantly.

Analyzing Morphological Properties of Early-Stage Toxic Amyloid β Oligomers by Atomic Force Microscopy.

Protein misfolding diseases, like Alzheimer's, Parkinson's, and Huntington's disease, are associated with misfolded protein aggregation. Alzheimer's disease is related to a progressive neuronal death induced by small amyloid β oligomers. Here, we describe the procedure to prepare and identify different types of small toxic amyloid β oligomers by atomic force microscopy (AFM).

Correction: Bimetallic nanocatalysts supported on graphitic carbon nitride for sustainable energy development: the shape-structure-activity relation.

[This corrects the article DOI: 10.1039/D0NA01063D.].

Bimetallic nanocatalysts supported on graphitic carbon nitride for sustainable energy development: the shape-structure-activity relation.

The catalytic performance of metal nanoparticles (NPs), including activity, selectivity, and durability, depends on their shape and structure at the molecular level. Consequently, metal NPs of different size and shape, , nanobelts, nanocubes, nanoflakes, and nanowires, demonstrate different reactivity and provide different reaction rates depending on the facet exposed. In this context, the present review aims to summarize the shape-structure-activity relation of metallic nanocatalysts.

Inhibition of Amyloid β-Induced Lipid Membrane Permeation and Amyloid β Aggregation by K162.

Alzheimer's disease (AD) is characterized by progressive neurodegeneration associated with amyloid β (Aβ) peptide aggregation. The aggregation of Aβ monomers (AβMs) leads to the formation of Aβ oligomers (AβOs), the neurotoxic Aβ form, capable of permeating the cell membrane. Here, we investigated the effect of a fluorene-based active drug candidate, named K162, on both Aβ aggregation and AβO toxicity toward the bilayer lipid membrane (BLM).

Alzheimer's disease-related amyloid β peptide causes structural disordering of lipids and changes the electric properties of a floating bilayer lipid membrane.

Neurodegeneration in Alzheimer's disease is associated with disruption of the neuronal cell membrane by the amyloid β (Aβ) peptide. However, the disruption mechanism and the resulting changes in membrane properties remain to be elucidated. To address this issue, herein the interaction of amyloid β monomers (AβMs) and amyloid β oligomers (AβOs) with a floating bilayer lipid membrane (fBLM) was studied using electrochemical and IR spectroscopy techniques.

Size-Dependent Interaction of Amyloid β Oligomers with Brain Total Lipid Extract Bilayer-Fibrillation Versus Membrane Destruction.

Amyloid β, Aβ(1-42), is a component of senile plaques present in the brain of Alzheimer's disease patients and one of the main suspects responsible for pathological consequences of the disease. Herein, we directly visualize the Aβ activity toward a brain-like model membrane and demonstrate that this activity strongly depends on the Aβ oligomer size. PeakForce quantitative nanomechanical mapping mode of atomic force microscopy imaging revealed that the interaction of large-size (LS) Aβ oligomers, corresponding to high-molecular-weight Aβ oligomers, with the brain total lipid extract (BTLE) membrane resulted in accelerated Aβ fibrillogenesis on the membrane surface.