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Автор: Grafiati
Опубліковано: 7 липня 2024
Оновлено: 7 липня 2024

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1

Chiorcea-Paquim, Ana-Maria, Teodor Adrian Enache, and Ana Maria Oliveira-Brett. "Electrochemistry of Alzheimer Disease Amyloid Beta Peptides." Current Medicinal Chemistry 25, no. 33 (October 24, 2018): 4066–83. http://dx.doi.org/10.2174/0929867325666180214112536.

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Alzheimer’s disease (AD) is a widespread form of dementia that is estimated to affect 44.4 million people worldwide. AD pathology is closely related to the accumulation of amyloid beta (Aβ) peptides in fibrils and plagues, the small oligomeric intermediate species formed during the Aβ peptides aggregation presenting the highest neurotoxicity. This review discusses the recent advances on the Aβ peptides electrochemical characterization. The Aβ peptides oxidation at a glassy carbon electrode occurs in one or two steps, depending on the amino acid sequence, length and content. The first electron transfer reaction corresponds to the tyrosine Tyr10 amino acid residue oxidation, and the second to all three histidine (His6, His13 and His14) and one methionine (Met35) amino acid residues. The Aβ peptides aggregation and amyloid fibril formation are electrochemically detected via the electroactive amino acids oxidation peak currents decrease that occurs in a time dependent manner. The Aβ peptides redox behaviour is correlated with changes in the adsorption morphology from initially random coiled structures, corresponding to the Aβ peptide monomers in random coil or in α-helix conformations, to aggregates, protofibrils and two types of fibrils, corresponding to the Aβ peptides in a β-sheet configuration, observed by atomic force microscopy. Electrochemical studies of Aβ peptides aggregation, mediated by the interaction with metal ions, particularly zinc, copper and iron, and different methodologies concerning the detection of Aβ peptide biomarkers of AD in biological fluids, using electrochemical biosensors, are also discussed.
2

Uéda, K., H. Fukushima, E. Masliah, Y. Xia, A. Iwai, M. Yoshimoto, D. A. Otero, J. Kondo, Y. Ihara, and T. Saitoh. "Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease." Proceedings of the National Academy of Sciences 90, no. 23 (December 1, 1993): 11282–86. http://dx.doi.org/10.1073/pnas.90.23.11282.

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A neuropathological hallmark of Alzheimer disease (AD) is a widespread amyloid deposition. We analyzed the entire amino acid sequences in an amyloid preparation and found, in addition to the major beta/A4-protein (A beta) fragment, two unknown peptides. We raised antibodies against synthetic peptides using subsequences of these peptides. These antibodies immunostained amyloid in neuritic and diffuse plaques as well as vascular amyloid. Electron microscopic analysis demonstrated that the immunostaining was localized on amyloid fibrils. We have isolated an apparently full-length cDNA encoding a 140-amino-acid protein within which two previously unreported amyloid sequences are encoded in tandem in the most hydrophobic domain. We tentatively named this 35-amino acid peptide NAC (non-A beta component of AD amyloid) and its precursor NACP. NAC is the second component, after A beta, identified chemically in the purified AD amyloid preparation. Secondary structure predictions indicate that the NAC peptide sequence has a strong tendency to form beta-structures consistent with its association with amyloid. NACP is detected as a M(r) 19,000 protein in the cytosolic fraction of brain homogenates and comigrates on immunoblots with NACP synthesized in Escherichia coli from NACP cDNA. NACP mRNA is expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver, suggesting its ubiquitous and brain-specific functions. The availability of the cDNA encoding full-length NACP should help to elucidate the mechanisms of amyloidosis in AD.
3

Ştefănescu, Raluca, Gabriela Dumitriṭa Stanciu, Andrei Luca, Ioana Cezara Caba, Bogdan Ionel Tamba та Cosmin Teodor Mihai. "Contributions of Mass Spectrometry to the Identification of Low Molecular Weight Molecules Able to Reduce the Toxicity of Amyloid-β Peptide to Cell Cultures and Transgenic Mouse Models of Alzheimer’s Disease". Molecules 24, № 6 (24 березня 2019): 1167. http://dx.doi.org/10.3390/molecules24061167.

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Alzheimer’s Disease affects approximately 33 million people worldwide and is characterized by progressive loss of memory at the cognitive level. The formation of toxic amyloid oligomers, extracellular amyloid plaques and amyloid angiopathy in brain by amyloid beta peptides are considered a part of the identified mechanism involved in disease pathogenesis. The optimal treatment approach leads toward finding a chemical compound able to form a noncovalent complex with the amyloid peptide thus blocking the process of amyloid aggregation. This direction gained an increasing interest lately, many studies demonstrating that mass spectrometry is a valuable method useful for the identification and characterization of such molecules able to interact with amyloid peptides. In the present review we aim to identify in the scientific literature low molecular weight chemical compounds for which there is mass spectrometric evidence of noncovalent complex formation with amyloid peptides and also there are toxicity reduction results which verify the effects of these compounds on amyloid beta toxicity towards cell cultures and transgenic mouse models developing Alzheimer’s Disease.
4

Jiang, H., D. Burdick, C. G. Glabe, C. W. Cotman, and A. J. Tenner. "beta-Amyloid activates complement by binding to a specific region of the collagen-like domain of the C1q A chain." Journal of Immunology 152, no. 10 (May 15, 1994): 5050–59. http://dx.doi.org/10.4049/jimmunol.152.10.5050.

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Abstract beta-amyloid peptides that accumulate within the brain of individuals with Alzheimer's disease bind to C1q and activate the classical C pathway via a specific interaction with a site within the collagen-like domain of C1q (C1q-CLF). Synthetic analogues of beta-amyloid peptides, beta 1-42 and beta 1-40, bound to C1q and were strong activators of C as assessed by both total C consumption and C4 consumption. beta 1-42 was significantly more effective than beta 1-40 in binding to C1q and triggering C activation, whereas beta 1-28 demonstrated little or no binding or C activation. This C-activating capacity seems to be largely correlated with the assembly of the beta 1-42 into low speed sedimentable aggregates and/or macromolecular fibrils. Radiolabeled C1q and C1q-CLF bind specifically to these aggregates or amyloid fibrils. In addition, using synthetic C1q peptides in a solid phase binding assay, the major binding site of beta 1-42 to C1q was localized to the C1q A chain collagen-like residues 14-26, a region previously described as a novel interaction site for Ab-independent activators of C1. C1q A chain peptide 14-26 blocked the ability of beta-amyloid peptides to activate the classical C pathway, providing evidence that this relatively unrecognized mechanism of C activation (via binding to the C1q-CLF) may have crucial physiologic consequences. Finally, these observations provide further support for the hypothesis that C activation and inflammation may be a component in the pathogenesis of AD and suggest possibilities for modulating the progression of AD.
5

Buneeva, O. A., O. V. Gnedenko, M. V. Medvedeva, A. S. Ivanov, and A. E. Medvedev. "The effect of neuroprotector isatin on binding of some model proteins with beta-amyloid peptide: a biosensor study." Biomeditsinskaya Khimiya 62, no. 6 (2016): 720–24. http://dx.doi.org/10.18097/pbmc20166206720.

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The amyloid-beta peptide 1-42 formed during proteolytic processing of the amyloid precursor protein (APP) plays a key role in the development or progression of Alzheimer's disease (AD) and other pathologies associated with formation of protein aggregates in the central nervous system. Recent proteomic profiling of mouse and rat brain preparations by means of beta-amyloid peptide immobilized on Affigel-10 revealed a large group of amyloid-binding proteins (n>80). Many (about 25%) of these proteins were previously identified as isatin-binding proteins. The aim of this study was to validate direct interaction between beta-amyloid peptide and highly purified intact and oxidized peroxiredoxin, M-type pyruvate kinase, alpha-enolase, and the effect of isatin on this interaction. The study performed using SPR-based Biacore 3000 and Biacore X100 biosensors has shown that all the proteins form molecular complexes with immobilized beta-amyloid peptide. The Kd values for these complexes varied from 8.36х10^-8 M (peroxiredoxin) to 1.97х10^-6 M (alpha-enolase). Oxidative modification of investigated proteins caused opposite effects on complexes of these peptides with beta-amyloid. The endogenous neuroprotector isatin increased dissociation of complexes formed by beta-amyloid peptide with both intact proteins (peroxiredoxin, glyceraldehyde-3-phosphate dehydrogenase) and/or oxidized proteins (peroxiredoxin, pyruvate kinase) used in this study.
6

Festa, Giulia, Francesco Mallamace, Giulia Maria Sancesario, Carmelo Corsaro, Domenico Mallamace, Enza Fazio, Laura Arcidiacono та ін. "Aggregation States of Aβ1–40, Aβ1–42 and Aβp3–42 Amyloid Beta Peptides: A SANS Study". International Journal of Molecular Sciences 20, № 17 (24 серпня 2019): 4126. http://dx.doi.org/10.3390/ijms20174126.

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Aggregation states of amyloid beta peptides for amyloid beta A β 1 – 40 to A β 1 – 42 and A β p 3 – 42 are investigated through small angle neutron scattering (SANS). The knowledge of these small peptides and their aggregation state are of key importance for the comprehension of neurodegenerative diseases (e.g., Alzheimer’s disease). The SANS technique allows to study the size and fractal nature of the monomers, oligomers and fibrils of the three different peptides. Results show that all the investigated peptides have monomers with a radius of gyration of the order of 10 Å, while the oligomers and fibrils display differences in size and aggregation ability, with A β p 3 – 42 showing larger oligomers. These properties are strictly related to the toxicity of the corresponding amyloid peptide and indeed to the development of the associated disease.
7

Mocanu, Cosmin Stefan, Marius Niculaua, Gheorghita Zbancioc, Violeta Mangalagiu та Gabi Drochioiu. "Novel Design of Neuropeptide-Based Drugs with β-Sheet Breaking Potential in Amyloid-Beta Cascade: Molecular and Structural Deciphers". International Journal of Molecular Sciences 23, № 5 (5 березня 2022): 2857. http://dx.doi.org/10.3390/ijms23052857.

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Our work discusses the investigation of 75 peptide-based drugs with the potential ability to break the β-sheet structures of amyloid-beta peptides from senile plaques. Hence, this study offers a unique insight into the design of neuropeptide-based drugs with β-sheet breaker potential in the amyloid-beta cascade for Alzheimer’s disease (AD). We started with five peptides (15QKLVFF20, 16KLVFF20, 17LVFF20, 16KLVF19 and 15QKLV18), to which 14 different organic acids were attached at the N-terminal. It was necessary to evaluate the physiochemical features of these sequences due to the biological correlation with our proposal. Hence, the preliminary analysis of different pharmacological features provided the necessary data to select the peptides with the best biocompatibility for administration purposes. Our approaches demonstrated that the peptides 17LVFF20, NA-17LVFF20, 16KLVF19 and NA-16KLVF19 (NA-nicotinic acid) have the ability to interfere with fibril formation and hence improve the neuro and cognitive functions. Moreover, the peptide conjugate NA-16KLVF19 possesses attractive pharmacological properties, demonstrated by in silico and in vitro studies. Tandem mass spectrometry showed no fragmentation for the spectra of 16KLVF19. Such important results suggest that under the action of protease, the peptide cleavage does not occur at all. Additionally, circular dichroism confirmed docking simulations and showed that NA-16KLVF19 may improve the β-sheet breaker mechanism, and thus the entanglement process of amyloid-beta peptides can be more effective.
8

Lee, Joo-Hee, Na-Hyun Ahn, Su-Bin Choi, Youngeun Kwon, and Seung-Hoon Yang. "Natural Products Targeting Amyloid Beta in Alzheimer’s Disease." International Journal of Molecular Sciences 22, no. 5 (February 26, 2021): 2341. http://dx.doi.org/10.3390/ijms22052341.

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Alzheimer’s disease (AD) is a neurodegenerative disease characterized by severe brain damage and dementia. There are currently few therapeutics to treat this disease, and they can only temporarily alleviate some of the symptoms. The pathogenesis of AD is mainly preceded by accumulation of abnormal amyloid beta (Aβ) aggregates, which are toxic to neurons. Therefore, modulation of the formation of these abnormal aggregates is strongly suggested as the most effective approach to treat AD. In particular, numerous studies on natural products associated with AD, aiming to downregulate Aβ peptides and suppress the formation of abnormal Aβ aggregates, thus reducing neural cell death, are being conducted. Generation of Aβ peptides can be prevented by targeting the secretases involved in Aβ-peptide formation (secretase-dependent). Additionally, blocking the intra- and intermolecular interactions of Aβ peptides can induce conformational changes in abnormal Aβ aggregates, whereby the toxicity can be ameliorated (structure-dependent). In this review, AD-associated natural products which can reduce the accumulation of Aβ peptides via secretase- or structure-dependent pathways, and the current clinical trial states of these products are discussed.
9

Miura, Yoshiko, Kiyofumi Yamamoto, Kikuko Yasuda, Yoshihiro Nishida, and Kazukiyo Kobayashi. "Inhibition of Alzheimer Amyloid Aggregation with Sulfate Glycopolymers." Advances in Science and Technology 57 (September 2008): 166–69. http://dx.doi.org/10.4028/www.scientific.net/ast.57.166.

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Glycopolymers carrying sulfate saccharides were found to suppress the formation of amyloid fibrils by amyloid beta peptides, as evaluated by fluorescence assay of thioflavin T and AFM. CD spectra showed that the conformation of amyloid beta peptides was changed from beta peptides depended on the glycopolymer additives, and that the glycopolymer additives reduced the β-sheet contents. Neutralization activity was confirmed by in vitro assay with HeLa cells. The sulfate group and the appropriate sugar contents were essential for the inhibitory effect.
10

Usui, Kenji, Shin-ichiro Yokota, Kazuya Iwata, and Yoshio Hamada. "Novel Purification Process for Amyloid Beta Peptide(1-40)." Processes 8, no. 4 (April 15, 2020): 464. http://dx.doi.org/10.3390/pr8040464.

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Amyloid beta peptide (Aβ)-related studies require an adequate supply of purified Aβ peptide. However, Aβ peptides are “difficult sequences” to synthesize chemically, and low yields are common due to aggregation during purification. Here, we demonstrate an easier synthesis, deprotection, reduction, cleavage, and purification process for Aβ(1-40) using standard 9-fluorenylmethyloxycarbonyl (Fmoc)-protected amino acids and solid-phase peptide synthesis (SPPS) resin [HMBA (4-hydroxymethyl benzamide) resin] that provides higher yields of Aβ(1-40) than previous standard protocols. Furthermore, purification requires a similar amount of time as conventional purification processes, although the peptide must be cleaved from the resin immediately prior to purification. The method described herein is not limited to the production of Aβ(1-40), and can be used to synthesize other easily-oxidized and aggregating sequences. Our proposed methodology will contribute to various fields using “difficult sequence” peptides, such as pharmaceutical and materials science, as well as research for the diagnosis and treatment of protein/peptide misfolding diseases.
11

Borutaite, Vilmante, Ramune Morkuniene, and Gintaras Valincius. "Beta-amyloid oligomers: recent developments." BioMolecular Concepts 2, no. 3 (June 1, 2011): 211–22. http://dx.doi.org/10.1515/bmc.2011.019.

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AbstractRecent studies point to a critical role of soluble β-amyloid oligomers in the pathogenesis of one of the most common neurodegenerative diseases, Alzheimer's disease (AD). Beta-amyloid peptides are cleavage products of a ubiquitously expressed protein, the amyloid precursor protein. Early studies suggested that accumulation of extracellular β-amyloid aggregates are the most toxic species causing synaptic dysfunction and neuronal loss in particular regions of the brain (neurobiological features underlying cognitive decline of the AD patients). In recent years, a shift of pardigm occurred, and now there is accumulating evidence that soluble oligomeric forms of the peptide are the most toxic to neuronal cells. In this review, we discuss recent findings on the toxic effects of amyloid-β oligomers, their physico-chemical properties and the possible pathways of their formation in vitro and in vivo.
12

Mehrazma, Banafsheh, Stanley Opare, Anahit Petoyan, and Arvi Rauk. "d-Amino Acid Pseudopeptides as Potential Amyloid-Beta Aggregation Inhibitors." Molecules 23, no. 9 (September 18, 2018): 2387. http://dx.doi.org/10.3390/molecules23092387.

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A causative factor for neurotoxicity associated with Alzheimer’s disease is the aggregation of the amyloid-β (Aβ) peptide into soluble oligomers. Two all d-amino acid pseudo-peptides, SGB1 and SGD1, were designed to stop the aggregation. Molecular dynamics (MD) simulations have been carried out to study the interaction of the pseudo-peptides with both Aβ13–23 (the core recognition site of Aβ) and full-length Aβ1–42. Umbrella sampling MD calculations have been used to estimate the free energy of binding, ∆G, of these peptides to Aβ13–23. The highest ∆Gbinding is found for SGB1. Each of the pseudo-peptides was also docked to Aβ1–42 and subjected up to seven microseconds of all atom molecular dynamics simulations. The resulting structures lend insight into how the dynamics of Aβ1–42 are altered by complexation with the pseudo-peptides and confirmed that SGB1 may be a better candidate for developing into a drug to prevent Alzheimer’s disease.
13

Ntarakas, Nikolaos, Inna Ermilova, and Alexander P. Lyubartsev. "Effect of lipid saturation on amyloid-beta peptide partitioning and aggregation in neuronal membranes: molecular dynamics simulations." European Biophysics Journal 48, no. 8 (October 26, 2019): 813–24. http://dx.doi.org/10.1007/s00249-019-01407-x.

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Abstract Aggregation of amyloid-$$\beta $$β (Aβ) peptides, cleaved from the amyloid precursor protein, is known as a precursor of the Alzheimer’s disease (AD). It is also known that Alzheimer’s disease is characterized by a substantial decrease of the amount of polyunsaturated lipids in the neuronal membranes of the frontal gray matter. To get insight into possible interconnection of these phenomena, we have carried out molecular dynamics simulations of two fragments of A$$\beta $$β peptide, A$$\beta $$β$$_{1-28}$$1-28 and A$$\beta $$β$$_{26-40}$$26-40, in four different lipid bilayers: two monocomponent ones (14:0-14:0 PC, 18:0-22:6 PC), and two bilayers containing mixtures of 18:0-18:0 PE, 22:6-22:6 PE, 16:0-16:0 PC and 18:1-18:1 PC lipids of composition mimicking neuronal membranes in a “healthy” and “AD” brain. The simulations showed that the presence of lipids with highly unsaturated 22:6cis fatty acids chains strongly affects the interaction of amyloid-$$\beta $$β peptides with lipid membranes. The polyunsaturated lipids cause stronger adsorption of A$$\beta $$β-peptides by the membrane and lead to weaker binding between peptides when the latter form aggregates. This difference in the behaviour observed in monocomponent bilayers is propagated in a similar fashion to the mixed membranes mimicking composition of neuronal membranes in “healthy” and “AD” brains, with “healthy” membrane having higher fraction of polyunsaturated lipids. Our simulations give strong indication that it can be physical–chemical background of the interconnection between amyloid fibrillization causing Alzheimer’s disease, and content of polyunsaturated lipids in the neuronal membranes.
14

Parkin, Edward T., Jessica E. Hammond, Lauren Owens, and Matthew D. Hodges. "The orphan drug dichloroacetate reduces amyloid beta-peptide production whilst promoting non-amyloidogenic proteolysis of the amyloid precursor protein." PLOS ONE 17, no. 1 (January 13, 2022): e0255715. http://dx.doi.org/10.1371/journal.pone.0255715.

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The amyloid cascade hypothesis proposes that excessive accumulation of amyloid beta-peptides is the initiating event in Alzheimer’s disease. These neurotoxic peptides are generated from the amyloid precursor protein via sequential cleavage by β- and γ-secretases in the ’amyloidogenic’ proteolytic pathway. Alternatively, the amyloid precursor protein can be processed via the ’non-amyloidogenic’ pathway which, through the action of the α-secretase a disintegrin and metalloproteinase (ADAM) 10, both precludes amyloid beta-peptide formation and has the additional benefit of generating a neuroprotective soluble amyloid precursor protein fragment, sAPPα. In the current study, we investigated whether the orphan drug, dichloroacetate, could alter amyloid precursor protein proteolysis. In SH-SY5Y neuroblastoma cells, dichloroacetate enhanced sAPPα generation whilst inhibiting β–secretase processing of endogenous amyloid precursor protein and the subsequent generation of amyloid beta-peptides. Over-expression of the amyloid precursor protein partly ablated the effect of dichloroacetate on amyloidogenic and non-amyloidogenic processing whilst over-expression of the β-secretase only ablated the effect on amyloidogenic processing. Similar enhancement of ADAM-mediated amyloid precursor protein processing by dichloroacetate was observed in unrelated cell lines and the effect was not exclusive to the amyloid precursor protein as an ADAM substrate, as indicated by dichloroacetate-enhanced proteolysis of the Notch ligand, Jagged1. Despite altering proteolysis of the amyloid precursor protein, dichloroacetate did not significantly affect the expression/activity of α-, β- or γ-secretases. In conclusion, dichloroacetate can inhibit amyloidogenic and promote non-amyloidogenic proteolysis of the amyloid precursor protein. Given the small size and blood-brain-barrier permeability of the drug, further research into its mechanism of action with respect to APP proteolysis may lead to the development of therapies for slowing the progression of Alzheimer’s disease.
15

Castano, E. M., F. Prelli, T. Wisniewski, A. Golabek, R. A. Kumar, C. Soto та B. Frangione. "Fibrillogenesis in Alzheimer's disease of amyloid β peptides and apolipoprotein E". Biochemical Journal 306, № 2 (1 березня 1995): 599–604. http://dx.doi.org/10.1042/bj3060599.

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A central event in Alzheimer's disease is the conformational change from normally circulating soluble amyloid beta peptides (A beta) and tau proteins into amyloid fibrils, in the form of senile plaques and neurofibrillary tangles respectively. The apolipoprotein E (apoE) gene locus has recently been associated with late-onset Alzheimer's disease. It is not know whether apoE plays a direct role in the pathogenesis of the disease. In the present work we have investigated whether apoE can affect the known spontaneous in vitro formation of amyloid-like fibrils by synthetic A beta analogues using a thioflavine-T assay for fibril formation, electron microscopy and Congo Red staining. Our results show that, under the conditions used, apoE directly promotes amyloid fibril formation, increasing both the rate of fibrillogenesis and the total amount of amyloid formed. ApoE accelerated fibril formation of both wild-type A beta-(1-40) and A beta-(1-40A), an analogue created by the replacement of valine with alanine at residue 18, which alone produces few amyloid-like fibrils. However, apoE produced only a minimal effect on A beta-(1-40Q), found in the Dutch variant of Alzheimer's disease. When recombinant apoE isoforms were used, apoE4 was more efficient than apoE3 at enhancing amyloid formation. These in vitro observations support the hypothesis that apoE acts as a pathological chaperone, promoting the beta-pleated-sheet conformation of soluble A beta into amyloid fibres, and provide a possible explanation for the association of the apoE4 genetic isoform with Alzheimer's disease.
16

Klunk, W. E., J. W. Pettegrew, and D. J. Abraham. "Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation." Journal of Histochemistry & Cytochemistry 37, no. 8 (August 1989): 1273–81. http://dx.doi.org/10.1177/37.8.2666510.

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The binding of Congo red to several purified amyloid-like peptides having a beta-pleated sheet conformation was quantitatively examined. Congo red binds preferentially to the beta-pleated sheet conformation of both insulin fibrils and poly-L-lysine. Congo red does not bind nearly so well to poly-L-serine or polyglycine, despite the fact that these peptides also have a beta-pleated sheet conformation. Binding to insulin fibrils was saturable with an apparent Bmax of 2 moles of Congo red per mole of insulin fibrils and an apparent KD of 1.75 x 10(-7) M. Binding to beta-poly-L-lysine was similar but had a much higher apparent Bmax of 43. Binding of Congo red to beta-poly-L-lysine was pH dependent and appeared to be determined by the number of protonated lysine residues in the 250 amino acid peptide. We present a new hypothesis in which Congo red binds to amyloid-like proteins via bonds between the two negatively charged sulfonic acid groups of Congo red and two positively charged amino acid residues of two separate protein molecules which are properly oriented by virtue of the beta-pleated sheet conformation of the peptide backbone.
17

Das, Utpal, Pallavi Manral, Brajesh Agrawal, Rao G. Hariprasad, Kolandaivelu Saravanan, Baskar Singh, Savita Yadav, Tej P. Singh, and Alagri Srinivasan. "P1-205 Amyloid beta peptide assembly: effect of antifibrillogenic peptides." Neurobiology of Aging 25 (July 2004): S154. http://dx.doi.org/10.1016/s0197-4580(04)80518-9.

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18

Linhananta, Apichart. "Free-Energy Landscape of Amyloid-Beta Peptides." Biophysical Journal 114, no. 3 (February 2018): 526a. http://dx.doi.org/10.1016/j.bpj.2017.11.2876.

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19

Parameshwaran, Kodeeswaran, Muralikrishnan Dhanasekaran, and Vishnu Suppiramaniam. "Amyloid beta peptides and glutamatergic synaptic dysregulation." Experimental Neurology 210, no. 1 (March 2008): 7–13. http://dx.doi.org/10.1016/j.expneurol.2007.10.008.

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20

Defrancesco, Michaela, Josef Marksteiner, and Christian Humpel. "Reduced beta-amyloid sensitivity for platelet–monocyte aggregates in EDTA blood of alzheimer patients." International Psychogeriatrics 30, no. 1 (August 17, 2017): 147–52. http://dx.doi.org/10.1017/s1041610217001612.

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ABSTRACTAlzheimer´s disease (AD) is a severe neurodegenerative brain disorder characterized by beta-amyloid plaques, Tau pathology, inflammation, neurodegeneration, and cerebrovascular dysfunction. Besides that, alterations in monocytes and platelets have been reported in the blood of Alzheimer patients. In the present study, we measured circulating levels of platelet–monocyte aggregates in EDTA blood of cognitively healthy participants and 40 AD patients, and examined their changes induced by stimulation with beta-amyloid peptides. We measured CD14, CD62P, and CD42a using fluorescence-activated cell scanning (FACS) analysis. Our data show that the levels of circulating monocyte–platelet aggregates were not different between healthy controls and AD patients. However, incubation with beta-amyloid-40, −42, and pyroglutamate-beta-amyloid increased the platelet–monocyte aggregation in healthy subjects, but not AD patients. Our data conclude that the interaction between monocytes and platelets is not altered in whole blood of AD patients, but their sensitivity toward beta-amyloid peptides is decreased. There might be a critical link between the interaction of platelets and monocytes in AD, which has to be explored in further studies.
21

Karine, B., G. Dupuis, E. H. Frost, and T. Fülöp. "AMYLOID BETA PEPTIDES AS ANTIMICROBIAL PEPTIDES: RELEVANCE FOR ALZHEIMER’S DISEASE?" Innovation in Aging 1, suppl_1 (June 30, 2017): 275. http://dx.doi.org/10.1093/geroni/igx004.1008.

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22

Mirgorodskaya, O. A., A. V. Protasov, Yu P. Kozmin, R. A. Bublyaev, and J. Gobom. "FEATURES OF MASS SPECTROMETRIC DETECTION BETA-AMYLOID PEPTIDES (ALZHEIMER'S PEPTIDES)." NAUCHNOE PRIBOROSTROENIE 32, no. 4 (November 20, 2022): 35–48. http://dx.doi.org/10.18358/np-32-4-i3548.

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Mass spectrometry combined with the use of isotope-labeled standards is one of the favored methods for the quantitative measurement of beta-amyloid concentrations in biological media. This article is devoted to the prevention of typical systematic errors in such measurements arising from the neglect of the possibility of beta-amyloid transformation into the denatured form, which gives in mass spectra signals three times more intensity than the native form. The degree of this denaturation was determined by the ability of the native form to set up a complex with α-2-macroglobulin. The denatured form lacks this point. It was shown that denaturation can occur in the case of heat treatment in an acidic environment or when DMSO is used as a solvent. Measurement error occurs when the isotope-labeled standard and the analyte are of different forms. There are suggested recommendations to overcome systematic errors in the quantitative analysis of these compounds by forcing denaturation of the mixture of the analyte with the standard before analysis.
23

Doytchinova, Irini, Mariyana Atanasova, Evdokiya Salamanova, Stefan Ivanov, and Ivan Dimitrov. "Curcumin Inhibits the Primary Nucleation of Amyloid-Beta Peptide: A Molecular Dynamics Study." Biomolecules 10, no. 9 (September 15, 2020): 1323. http://dx.doi.org/10.3390/biom10091323.

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The amyloid plaques are a key hallmark of neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease. Amyloidogenesis is a complex long-lasting multiphase process starting with the formation of nuclei of amyloid peptides: a process assigned as a primary nucleation. Curcumin (CU) is a well-known inhibitor of the aggregation of amyloid-beta (Aβ) peptides. Even more, CU is able to disintegrate preformed Aβ firbils and amyloid plaques. Here, we simulate by molecular dynamics the primary nucleation process of 12 Aβ peptides and investigate the effects of CU on the process. We found that CU molecules intercalate among the Aβ chains and bind tightly to them by hydrogen bonds, hydrophobic, π–π, and cation–π interactions. In the presence of CU, the Aβ peptides form a primary nucleus of a bigger size. The peptide chains in the nucleus become less flexible and more disordered, and the number of non-native contacts and hydrogen bonds between them decreases. For comparison, the effects of the weaker Aβ inhibitor ferulic acid (FA) on the primary nucleation are also examined. Our study is in good agreement with the observation that taken regularly, CU is able to prevent or at least delay the onset of neurodegenerative disorders.
24

Airoldi, Cristina, Francisco Cardona, Erika Sironi, Laura Colombo, Mario Salmona, Ilaria Cambianica, Francesca Ornaghi, Giulio Sancini, Francesco Nicotra, and Barbara La Ferla. "Fluorescent amyloid β-peptide ligand derivatives as potential diagnostic tools for Alzheimer’s disease." Pure and Applied Chemistry 85, no. 9 (September 1, 2013): 1813–23. http://dx.doi.org/10.1351/pac-con-12-11-07.

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Aβ-peptide ligands based on a cis-glycofused benzopyran structure have been fluorescently labeled using coumarine derivatives. Among the synthesized compounds, two conserved their binding ability to β-amyloid peptides, as shown by NMR experiments. Moreover, exploiting its fluorescent property, it was demonstrated that one of such compounds was able to cross an in vitro model of blood–brain barrier (BBB) and to stain Aβ‑deposits.
25

Kucheryavykh, Lilia Y., Jescelica Ortiz-Rivera, Yuriy V. Kucheryavykh, Astrid Zayas-Santiago, Amanda Diaz-Garcia, and Mikhail Y. Inyushin. "Accumulation of Innate Amyloid Beta Peptide in Glioblastoma Tumors." International Journal of Molecular Sciences 20, no. 10 (May 20, 2019): 2482. http://dx.doi.org/10.3390/ijms20102482.

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Immunostaining with specific antibodies has shown that innate amyloid beta (Aβ) is accumulated naturally in glioma tumors and nearby blood vessels in a mouse model of glioma. In immunofluorescence images, Aβ peptide coincides with glioma cells, and enzyme-linked immunosorbent assay (ELISA) have shown that Aβ peptide is enriched in the membrane protein fraction of tumor cells. ELISAs have also confirmed that the Aβ(1–40) peptide is enriched in glioma tumor areas relative to healthy brain areas. Thioflavin staining revealed that at least some amyloid is present in glioma tumors in aggregated forms. We may suggest that the presence of aggregated amyloid in glioma tumors together with the presence of Aβ immunofluorescence coinciding with glioma cells and the nearby vasculature imply that the source of Aβ peptides in glioma can be systemic Aβ from blood vessels, but this question remains unresolved and needs additional studies.
26

Barden, C., F. Meier-Stephenson, MD Carter, S. Banfield, EC Diez, B. Kelly, E. Lu, et al. "Design and development of drugs for Alzheimer’s dementia as a protein misfolding disorder." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 42, S1 (May 2015): S16. http://dx.doi.org/10.1017/cjn.2015.95.

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Background: There are no disease modifying agents for the treatment of Alzheimer’s disease (AD). Pathologically, AD is associated with the misfolding of two peptides: beta-amyloid (plaques) and tau (tangles). Methods: Using large-scale computer simulations, we modelled the misfolding of both beta-amyloid and tau, identifying a common conformational motif (CCM; i.e. an abnormal peptide shape), present in both beta-amyloid and tau, that promotes their misfolding. We screened a library of 11.8 million compounds against this in silico model of protein misfolding, identifying three novel molecular classes of putative therapeutics as anti-protein misfolding agents. We synthesized approximately 400 new chemical entity drug-like molecules in each of these three classes (i.e. 1200 potential drug candidates). These were comprehensively screened in a battery of five in vitro protein oligomerization assays. Selected compounds were next evaluated in the APP/PS1 doubly transgenic mouse model of AD. Results: Two new classes of molecules were identified with the ability to block the oligomerization of both beta-amyloid and tau. These compounds are drug-like with good pharmacokinetic properties and are brain-penetrant. They exhibit excellent efficacy in transgenic mouse models. Conclusion: Computer aided drug design has enabled the discovery of novel drug-like molecules able to inhibit both tau and beta-amyloid misfolding.
27

Eckenhoff, Roderic G., Jonas S. Johansson, Huafeng Wei, Anna Carnini, Baobin Kang, Wenlin Wei, Ravindernath Pidikiti, Jason M. Keller та Maryellen F. Eckenhoff. "Inhaled Anesthetic Enhancement of Amyloid-β Oligomerization and Cytotoxicity". Anesthesiology 101, № 3 (1 вересня 2004): 703–9. http://dx.doi.org/10.1097/00000542-200409000-00019.

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Background The majority of surgical patients receive inhaled anesthetics, principally small haloalkanes and haloethers. Long-term cognitive problems occur in the elderly subsequent to anesthesia and surgery, and previous surgery might also be a risk factor for neurodegenerative disorders like Alzheimer and Parkinson disease. The authors hypothesize that inhaled anesthetics contribute to these effects through a durable enhancement of peptide oligomerization. Methods Light scattering, filtration assays, electron microscopy, fluorescence spectroscopy and size-exclusion chromatography was used to characterize the concentration-dependent effects of halothane, isoflurane, propofol, and ethanol on amyloid beta peptide oligomerization. Pheochromocytoma cells were used to characterize cytotoxicity of amyloid oligomers with and without the above anesthetics. Results Halothane and isoflurane enhanced amyloid beta oligomerization rates and pheochromocytoma cytotoxicity in vitro through a preference for binding small oligomeric species. Ethanol and propofol inhibited oligomerization at low concentration but enhanced modestly at very high concentration. Neither ethanol nor propofol enhanced amyloid beta toxicity in pheochromocytoma cells. Conclusions Inhaled anesthetics enhance oligomerization and cytotoxicity of Alzheimer disease-associated peptides. In addition to the possibility of a general mechanism for anesthetic neurotoxicity, these results call for further evaluation of the interaction between neurodegenerative disorders, dementia, and inhalational anesthesia.
28

Sun, Albert Y., Bozena Draczynska-Lusiak, and Grace Y. Sun. "Oxidized lipoproteins, beta amyloid peptides and alzheimer’s disease." Neurotoxicity Research 3, no. 2 (March 2001): 167–78. http://dx.doi.org/10.1007/bf03033189.

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29

Tzaferis, John, Margaret Racke, Theresa Day, and Ronald DeMattos. "P4-297: Standardization of beta-amyloid reference peptides." Alzheimer's & Dementia 9 (July 2013): P813. http://dx.doi.org/10.1016/j.jalz.2013.05.1690.

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30

Fülöp, Lívia, Botond Penke, and Márta Zarándi. "Synthesis and fluorescent labeling of beta-amyloid peptides." Journal of Peptide Science 7, no. 8 (July 17, 2001): 397–401. http://dx.doi.org/10.1002/psc.346.

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31

Gutiérrez-Lerma, Armando I., Benito Ordaz, and Fernando Peña-Ortega. "Amyloid Beta Peptides Differentially Affect Hippocampal Theta Rhythms In Vitro." International Journal of Peptides 2013 (June 25, 2013): 1–11. http://dx.doi.org/10.1155/2013/328140.

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Soluble amyloid beta peptide (Aβ) is responsible for the early cognitive dysfunction observed in Alzheimer's disease. Both cholinergically and glutamatergically induced hippocampal theta rhythms are related to learning and memory, spatial navigation, and spatial memory. However, these two types of theta rhythms are not identical; they are associated with different behaviors and can be differentially modulated by diverse experimental conditions. Therefore, in this study, we aimed to investigate whether or not application of soluble Aβ alters the two types of theta frequency oscillatory network activity generated in rat hippocampal slices by application of the cholinergic and glutamatergic agonists carbachol or DHPG, respectively. Due to previous evidence that oscillatory activity can be differentially affected by different Aβ peptides, we also compared Aβ25−35 and Aβ1−42 for their effects on theta rhythms in vitro at similar concentrations (0.5 to 1.0 μM). We found that Aβ25−35 reduces, with less potency than Aβ1−42, carbachol-induced population theta oscillatory activity. In contrast, DHPG-induced oscillatory activity was not affected by a high concentration of Aβ25−35 but was reduced by Aβ1−42. Our results support the idea that different amyloid peptides might alter specific cellular mechanisms related to the generation of specific neuronal network activities, instead of exerting a generalized inhibitory effect on neuronal network function.
32

Kouza, M., A. Banerji, A. Kolinski, I. A. Buhimschi, and A. Kloczkowski. "Oligomerization of FVFLM peptides and their ability to inhibit beta amyloid peptides aggregation: consideration as a possible model." Physical Chemistry Chemical Physics 19, no. 4 (2017): 2990–99. http://dx.doi.org/10.1039/c6cp07145g.

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33

Lin, Yen-Ling, Yu-Sheng Cheng, Cheng-I. Ho, Zhong-Hong Guo, Shing-Jong Huang, Mai-Liis Org, Andres Oss, Ago Samoson, and Jerry Chun Chung Chan. "Preparation of fibril nuclei of beta-amyloid peptides in reverse micelles." Chemical Communications 54, no. 74 (2018): 10459–62. http://dx.doi.org/10.1039/c8cc05882b.

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34

Radko, S. P., S. A. Khmeleva, E. V. Suprun, S. A. Kozin, N. V. Bodoev, A. A. Makarov, A. I. Archakov, and V. V. Shumyantseva. "Physico-chemical methods for studing beta-amyloid aggregation." Biomeditsinskaya Khimiya 61, no. 2 (2015): 203–18. http://dx.doi.org/10.18097/pbmc20156102203.

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Alzheimer's disease is the most prevalent neurodegenerative pathology. According to the amyloid cascade hypothesis, a key event of the Alzheimer's disease pathogenesis is a transition of the b-amyloid peptide (Аb) from the monomeric form to the aggregated state. The mechanism of Аb aggregation is intensively studied in vitro, by means of synthetic peptides and various physico-chemical methods allowing evaluation of size, molecular structure, and morphology of the formed aggregates. The paper reviews both the well-known and recently introduced physico-chemical methods for analysis of Аb aggregation, including microscopу, optical and fluorescent methods, method of electron paramagnetic resonance, electrochemical and electrophoretic methods, gel-filtration, and mass spectrometric methods. Merits and drawbacks of the methods are discussed. The unique possibility to simultaneously observe Аb monomers as well oligomers and large aggregates by means of atomic force microscopy or fluorescence correlation spectroscopy is emphasized. The high detection sensitivity of the latter method, monitoring the aggregation process in Аb solutions at low peptide concentrations is underlined. Among mass spectrometric methods, the ion mobility mass spectrometry is marked out as a method enabling to obtain information about both the spectrum of Аb oligomers and their structure. It is pointed out that the use of several methods giving the complementary data about Аb aggregates is the best experimental approach to studying the process of b-amyloid peptide aggregation in vitro.
35

Nawrot, Barbara. "Targeting BACE with small inhibitory nucleic acids - a future for Alzheimer's disease therapy?" Acta Biochimica Polonica 51, no. 2 (June 30, 2004): 431–44. http://dx.doi.org/10.18388/abp.2004_3582.

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beta-Secretase, a beta-site amyloid precursor protein (APP) cleaving enzyme (BACE), participates in the secretion of beta-amyloid peptides (Abeta), the major components of the toxic amyloid plaques found in the brains of patients with Alzheimer's disease (AD). According to the amyloid hypothesis, accumulation of Abeta is the primary influence driving AD pathogenesis. Lowering of Abeta secretion can be achieved by decreasing BACE activity rather than by down-regulation of the APP substrate protein. Therefore, beta-secretase is a primary target for anti-amyloid therapeutic drug design. Several approaches have been undertaken to find an effective inhibitor of human beta-secretase activity, mostly in the field of peptidomimetic, non-cleavable substrate analogues. This review describes strategies targeting BACE mRNA recognition and its down-regulation based on the antisense action of small inhibitory nucleic acids (siNAs). These include antisense oligonucleotides, catalytic nucleic acids - ribozymes and deoxyribozymes - as well as small interfering RNAs (siRNAs). While antisense oligonucleotides were first used to identify an aspartyl protease with beta-secretase activity, all the strategies now demonstrate that siNAs are able to inhibit BACE gene expression in a sequence-specific manner, measured both at the level of its mRNA and at the level of protein. Moreover, knock-down of BACE reduces the intra- and extracellular population of Abeta40 and Abeta42 peptides. An anti-amyloid effect of siNAs is observed in a wide spectrum of cell lines as well as in primary cortical neurons. Thus targeting BACE with small inhibitory nucleic acids may be beneficial for the treatment of Alzheimer's disease and for future drug design.
36

Jalkute, Chidambar B., Sagar H. Barage та Kailas D. Sonawane. "Insight into molecular interactions of Aβ peptide and gelatinase from Enterococcus faecalis: a molecular modeling approach". RSC Advances 5, № 14 (2015): 10488–96. http://dx.doi.org/10.1039/c4ra09354b.

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37

Lichti, Cheryl, Anthony N. Vomund, Orion J. Peterson, Xiaoxiao Wan, and Emil R. Unanue. "Analysis of the nonobese diabetic mouse islet MHC-II peptidome reveals posttranslationally modified autoantigens." Journal of Immunology 204, no. 1_Supplement (May 1, 2020): 142.12. http://dx.doi.org/10.4049/jimmunol.204.supp.142.12.

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Abstract Autoimmune diabetes results from the destruction of insulin-producing beta cells, a process initiated by CD4 T cells recognizing MHC-II bound beta cell-derived peptides. We identified MHC-II bound peptides in the islets and throughout the peripheral lymphatic system in order to better understand diabetes initiation and progression. Toward this end, we performed unbiased nanoflow liquid chromatography-tandem mass spectrometry (nLC-MS/MS) analysis to obtain sequence information for MHC-II peptides isolated from islets, pancreatic lymph nodes and spleens of nonobese diabetic (NOD) mice. Peptides derived from beta cell proteins were further examined for their relative I-Ag7 binding strength and CD4 T cell autoreactivity. For a discussion of the major immunogenic peptides derived from the B chain of insulin and from C peptide, see the abstract of Wan et al. Herein we discuss the finding of a deamidated C peptide fragment and our search for fused peptides. We identified the deamidated insulin-1 C peptide fragment Ins1C:51–61, LQTLALEVARE. Evidence in the literature supports this C-terminal deamidation as being spontaneous rather than enzyme-mediated. Deamidation improved I-Ag7 binding compared to the wild type peptide and increased its immunogenicity, demonstrating the biological importance of this modification. The homologous peptide from insulin-2 was not identified, indicating a possible sequence bias for spontaneous deamidation. We identified only one fused peptide bound to I-Ag7, an insulin C peptide-islet amyloid polypeptide hybrid insulin peptide (HIP) that matches the previously reported HIP6.9. We also identified several free fused peptides in crinosomes and posit this as the probable site of their formation.
38

Tillett, Khalilia C., та Juan R. Del Valle. "N-Amino peptide scanning reveals inhibitors of Aβ42 aggregation". RSC Advances 10, № 24 (2020): 14331–36. http://dx.doi.org/10.1039/d0ra02009e.

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39

Stańczykiewicz, Bartłomiej, Tomasz M. Goszczyński, Paweł Migdał, Marta Piksa, Krzysztof Pawlik, Jakub Gburek, Krzysztof Gołąb, Bogusława Konopska та Agnieszka Zabłocka. "Effect of Ovocystatin on Amyloid β 1-42 Aggregation—In Vitro Studies". International Journal of Molecular Sciences 24, № 6 (12 березня 2023): 5433. http://dx.doi.org/10.3390/ijms24065433.

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Amyloid β peptides (Aβ) aggregating in the brain have a potential neurotoxic effect and are believed to be a major cause of Alzheimer’s disease (AD) development. Thus, inhibiting amyloid polypeptide aggregation seems to be a promising approach to the therapy and prevention of this neurodegenerative disease. The research presented here is directed at the determination of the inhibitory activity of ovocystatin, the cysteine protease inhibitor isolated from egg white, on Aβ42 fibril genesis in vitro. Thioflavin-T (ThT) assays, which determine the degree of aggregation of amyloid peptides based on fluorescence measurement, circular dichroism spectroscopy (CD), and transmission electron microscopy (TEM) have been used to assess the inhibition of amyloid fibril formation by ovocystatin. Amyloid beta 42 oligomer toxicity was measured using the MTT test. The results have shown that ovocystatin possesses Aβ42 anti-aggregation activity and inhibits Aβ42 oligomer toxicity in PC12 cells. The results of this work may help in the development of potential substances able to prevent or delay the process of beta-amyloid aggregation—one of the main reasons for Alzheimer’s disease.
40

Adaya-Villanueva, Alvaro, Benito Ordaz, Hugo Balleza-Tapia, Abraham Márquez-Ramos, and Fernando Peña-Ortega. "Beta-like hippocampal network activity is differentially affected by amyloid beta peptides." Peptides 31, no. 9 (September 2010): 1761–66. http://dx.doi.org/10.1016/j.peptides.2010.06.003.

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41

Nakagawa, Kazuhiro, Shinobu Kitazume, Ritsuko Oka, Kei Maruyama, Takaomi C. Saido, Yuji Sato, Tamao Endo, and Yasuhiro Hashimoto. "Sialylation enhances the secretion of neurotoxic amyloid-beta peptides." Journal of Neurochemistry 96, no. 4 (February 2006): 924–33. http://dx.doi.org/10.1111/j.1471-4159.2005.03595.x.

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42

Khandogin, J., and C. L. Brooks. "Linking folding with aggregation in Alzheimer's beta-amyloid peptides." Proceedings of the National Academy of Sciences 104, no. 43 (October 17, 2007): 16880–85. http://dx.doi.org/10.1073/pnas.0703832104.

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43

Gouras, G. K., H. Xu, R. S. Gross, J. P. Greenfield, B. Hai, R. Wang, and P. Greengard. "Testosterone reduces neuronal secretion of Alzheimer's beta -amyloid peptides." Proceedings of the National Academy of Sciences 97, no. 3 (February 1, 2000): 1202–5. http://dx.doi.org/10.1073/pnas.97.3.1202.

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44

Bisok, Anna, Marietta Koźlarek, Anna Burwiel, Julia Telus, Joanna M. Wolak, Żaneta Polańska, and Maciej Kozak. "Studies of selected carbon nanomaterials with amyloid beta peptides." Biophysical Journal 122, no. 3 (February 2023): 349a. http://dx.doi.org/10.1016/j.bpj.2022.11.1939.

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45

Enache, Teodor Adrian, and Ana Maria Oliveira-Brett. "Alzheimer's disease amyloid beta peptides in vitro electrochemical oxidation." Bioelectrochemistry 114 (April 2017): 13–23. http://dx.doi.org/10.1016/j.bioelechem.2016.11.003.

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46

Galante, D., E. Cavallo, A. Perico, and C. D'Arrigo. "Effect of ferric citrate on amyloid-beta peptides behavior." Biopolymers 109, no. 6 (June 2018): e23224. http://dx.doi.org/10.1002/bip.23224.

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47

WOOD, W., F. SCHROEDER, U. IGBAVBOA, N. AVDULOV, and S. CHOCHINA. "Brain membrane cholesterol domains, aging and amyloid beta-peptides." Neurobiology of Aging 23, no. 5 (September 2002): 685–94. http://dx.doi.org/10.1016/s0197-4580(02)00018-0.

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48

Maleeff, Beverly E., Timothy K. Hart, Stephen J. Wood, and Ronald Wetzel. "Effect of pH and inhibitors on beta-amyloid fibril assembly." Proceedings, annual meeting, Electron Microscopy Society of America 54 (August 11, 1996): 752–53. http://dx.doi.org/10.1017/s0424820100166221.

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Alzheimer's disease is characterized post-mortem in part by abnormal extracellular neuritic plaques found in brain tissue. There appears to be a correlation between the severity of Alzheimer's dementia in vivo and the number of plaques found in particular areas of the brain. These plaques are known to be the deposition sites of fibrils of the protein β-amyloid. It is thought that if the assembly of these plaques could be inhibited, the severity of the disease would be decreased. The peptide fragment Aβ, a precursor of the p-amyloid protein, has a 40 amino acid sequence, and has been shown to be toxic to neuronal cells in culture after an aging process of several days. This toxicity corresponds to the kinetics of in vitro amyloid fibril formation. In this study, we report the biochemical and ultrastructural effects of pH and the inhibitory agent hexadecyl-N-methylpiperidinium (HMP) bromide, one of a class of ionic micellar detergents known to be capable of solubilizing hydrophobic peptides, on the in vitro assembly of the peptide fragment Aβ.
49

Ayoubi, Riham, Maryam Fotouhi, Donovan Worrall, Kathleen Southern, and Carl Laflamme. "Identification of high-performing antibodies for amyloid-beta precursor protein for use in Western Blot, immunoprecipitation and immunofluorescence." F1000Research 12 (August 9, 2023): 956. http://dx.doi.org/10.12688/f1000research.139867.1.

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The amyloid-beta precursor protein is a transmembrane protein expressed in many tissues and highly concentrated in the brain. The protein is of significant interest due to its involvement in the generation of amyloidogenic β-amyloid peptides, prone to plaque formation that is characteristic of Alzheimer’s Disease. The scientific community would benefit from the availability of high-quality anti-amyloid-beta precursor protein antibodies to enhance reproducible research on this target. In this study, we characterized eleven amyloid-beta precursor protein commercial antibodies for Western blot, immunoprecipitation, and immunofluorescence using a standardized experimental protocol based on comparing read-outs in knockout cell lines and isogenic parental controls. We identified many high-performing antibodies and encourage readers to use this report as a guide to select the most appropriate antibody for their specific needs.
50

Oberoi, Pankaj, Robert Umek, Nyssa Puskar, Jill Dunty, Leonid Dzantiev, David Stewart, and Jacob Wohlstadter. "P1-207: Quantification of higher order forms of beta-amyloid and total beta-amyloid peptides in CSF." Alzheimer's & Dementia 9 (July 2013): P228. http://dx.doi.org/10.1016/j.jalz.2013.05.431.

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