Amyloid β-peptides 1–40 and 1–42 form oligomers with mixed β-sheets

Baldassarre, Maurizio; Baronio, Cesare M.; Morozova‐Roche, Ludmilla A.; Barth, Andreas

doi:10.1039/c7sc01743j

Cited by 36 publications

(53 citation statements)

References 51 publications

(60 reference statements)

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“…Experimental procedures were as described previously. 65 Briefly, hexafluoroisopropanol-(HFIP) treated Ab was dissolved in 20 mM NaO 2 H in order to obtain a monomeric peptide solution at a concentration of 200 mM. Unlabeled and labeled peptides were mixed and 4 mL of this solution added to a dry film produced from 4 mL of 100 mM sodium phosphate to bring the solution to p 2 H 7.4 and initiate aggregation.…”

Section: Methodsmentioning

confidence: 99%

“…It produced small-sized oligomers for Ab 40 and Ab 42 and additional larger aggregates for Ab 42 as shown by gel electrophoresis of photo-crosslinked samples. 65 The peptide solution was placed between two CaF 2 windows that were separated by a 50 mm plastic spacer. FTIR spectra were recorded approximately 20 min after initiation of aggregation with a Tensor 37 FTIR spectrometer (Bruker, Germany) that was equipped with a sample shutter.…”

Section: Methodsmentioning

confidence: 99%

“…Thus, mixing of different carbon isotopes in a b-sheet leads to a downshift of the high wavenumber band and an upshift of the low wavenumber band which decreases the splitting between the two bands. 65 Using a combination of isotope-edited FTIR spectroscopy and spectrum calculation, we have found that mixtures of monomeric Ab 40 and Ab 42 form mixed hetero-oligomers. 65 This work is here extended to homo-oligomers of either Ab 40 or Ab 42 .…”

Section: Introductionmentioning

confidence: 99%

“…65 Using a combination of isotope-edited FTIR spectroscopy and spectrum calculation, we have found that mixtures of monomeric Ab 40 and Ab 42 form mixed hetero-oligomers. 65 This work is here extended to homo-oligomers of either Ab 40 or Ab 42 . In particular, we describe calculations that aimed to achieve a quantitative agreement with the experiments.…”

Section: Introductionmentioning

confidence: 99%

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Insight into the internal structure of amyloid-β oligomers by isotope-edited Fourier transform infrared spectroscopy

Baronio

Baldassarre

Barth

2019

Phys. Chem. Chem. Phys.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Insight into the internal structure of amyloid-β oligomers by isotope-edited Fourier transform infrared spectroscopy

Baronio

Baldassarre

Barth

2019

Phys. Chem. Chem. Phys.

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“…Two-to four-fold increases of basal production were measured in response to the bacterial endotoxin (LPS), used in the concentration range of 10-5000 ng/ml [48]. Similarly, the Aβ 1-40 peptide, another peptide involved in the Alzheimer's disease pathogenesis [49], induced a two-fold increase of basal IL-6 production at 10 μM and a 10-12-fold increase at 20-60 μM. The effects of Aβ 1-40 were selective on the IL-6 pathway, and the secretion of other inflammatory mediators (i.e., TNFα, IL-1α, IL-1β, and caspase-1) was not modified [47].…”

Section: Functional Properties Cytokine and Chemokine Productionmentioning

confidence: 99%

The human microglial HMC3 cell line: where do we stand? A systematic literature review

Russo

Cappoli

Coletta

et al. 2018

J Neuroinflammation

163

130

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Microglia, unique myeloid cells residing in the brain parenchyma, represent the first line of immune defense within the central nervous system. In addition to their immune functions, microglial cells play an important role in other cerebral processes, including the regulation of synaptic architecture and neurogenesis. Chronic microglial activation is regarded as detrimental, and it is considered a pathogenic mechanism common to several neurological disorders. Microglial activation and function have been extensively studied in rodent experimental models, whereas the characterization of human cells has been limited due to the restricted availability of primary sources of human microglia. To overcome this problem, human immortalized microglial cell lines have been developed. The human microglial clone 3 cell line, HMC3, was established in 1995, through SV40-dependent immortalization of human embryonic microglial cells. It has been recently authenticated by the American Type Culture Collection (ATCC®) and distributed under the name of HMC3 (ATCC®CRL-3304). The HMC3 cells have been used in six research studies, two of which also indicated by ATCC® as reference articles. However, a more accurate literature revision suggests that clone 3 was initially distributed under the name of CHME3. In this regard, several studies have been published, thus contributing to a more extensive characterization of this cell line. Remarkably, the same cell line has been used in different laboratories with other denominations, i.e., CHME-5 cells and C13-NJ cells. In view of the fact that “being now authenticated by ATCC®” may imply a wider distribution of the cells, we aimed at reviewing data obtained with the human microglia cell line clone 3, making the readers aware of this complicated nomenclature. In addition, we also included original data, generated in our laboratory with the HMC3 (ATCC®CRL-3304) cells, providing information on the current state of the culture together with supplementary details on the culturing procedures to obtain and maintain viable cells.

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Heterotypic Seeding Generates Mixed Amyloid Polymorphs

Banerjee,

Baghel,

Edmonds

et al. 2024

Small Science

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Aggregation of the amyloid β (Aβ) peptide into fibrils represents one of the major biochemical pathways underlying the development of Alzheimer's disease (AD). Extensive studies have been carried out to understand the role of fibrillar seeds on the overall kinetics of amyloid aggregation. However, the precise effect of seeds that are structurally or sequentially different from Aβ on the structure of the resulting amyloid aggregates is yet to be fully understood. Herein, nanoscale infrared spectroscopy is used to probe the spectral facets of individual aggregates formed by aggregating Aβ42 with antiparallel fibrillar seeds of Aβ(16–22) and E22Q Aβ(1–40) Dutch mutant and it is demonstrated that Aβ can form heterotypic or mixed polymorphs that deviate significantly from its expected parallel cross β structure. It is further shown that the formation of heterotypic aggregates is not limited to the coaggregation of Aβ and its isomers, and that the former can form heterotypic fibrils with alpha‐synuclein and brain protein lysates. These findings highlight the complexity of Aβ aggregation in AD and underscore the need to explore how Aβ interacts with other brain components, which is crucial for developing better therapeutic strategies for AD.

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Amyloid β-peptides 1–40 and 1–42 form oligomers with mixed β-sheets

Abstract: Aβ40 and Aβ42 co-aggregate and form oligomers with mixed β-sheets as revealed by isotope-edited infrared spectroscopy.

Cited by 36 publications

References 51 publications

Insight into the internal structure of amyloid-β oligomers by isotope-edited Fourier transform infrared spectroscopy

Insight into the internal structure of amyloid-β oligomers by isotope-edited Fourier transform infrared spectroscopy

The human microglial HMC3 cell line: where do we stand? A systematic literature review

Heterotypic Seeding Generates Mixed Amyloid Polymorphs

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