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Journal articles on the topic 'Amyloid-beta peptide (A-beta)'

Author: Grafiati

Published: 9 March 2023

Last updated: 31 July 2025

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1

Muhammad, Jehangir, Wang Xiaohui, Zhao Ye, Ali Umar, kasmiri Kashif, and cheng Wang. "Inhibition of amyloid beta oligomer, fibrils, and peptide using nanoparticles to disrupt Alzheimer's pathogenesis." World Journal of Advanced Research and Reviews 23, no. 2 (2024): 343–57. https://doi.org/10.5281/zenodo.14836935.

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The Aβ peptide, which is connected to the development of Alzheimer's disease, forms highly neurotoxic prefibrillar oligomeric aggregates, which are challenging to study due to their fleeting, low prevalence, and diverse nature. These aggregates are considered to play a role in the pathogenesis of numerous neurodegenerative diseases. The potential approach of blocking or disrupting the buildup of amyloid peptides, particularly amyloid-β (AβOs), by using nanoparticles that specifically bind or prevent their aggregation to develop new medications and treatments for Alzheimer's dise

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2

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 di

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3

Aloufi, Bandar. "Molecular dynamics simulation analysis of the beta amyloid peptide with docked inhibitors." Bioinformation 18, no. 7 (2022): 622–29. http://dx.doi.org/10.6026/97320630018622.

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Beta amyloid peptide is widely studied due to its association with Alzheimer disease (AD). Various study reported that the accumulation of beta amyloid in brain cells leads to Alzheimer disease. Hence, Beta amyloid peptide could be a potential target of anti-AD therapy. Hence, it is of interest to develop potent inhibitors for Beta amyloid peptide in the context of Alzheimer disease (AD). We report the binding features of Ascorbic acid, Cysteine, Dithioerythriol, Dithiothreitol, Malic acid and α-Tocopherol with beta amyloid having binding energy values of -6.7, -6.5, -6.0, -6.5, -6.7 and - 7.0

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4

Uéda, K., H. Fukushima, E. Masliah, et al. "Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease." Proceedings of the National Academy of Sciences 90, no. 23 (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

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5

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 (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-a

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6

Muhammad Jehangir, Xiaohui Wang, Ye Zhao, Umar Ali, Kashif kasmiri, and Wang cheng. "Inhibition of amyloid beta oligomer, fibrils, and peptide using nanoparticles to disrupt Alzheimer's pathogenesis." World Journal of Advanced Research and Reviews 23, no. 2 (2024): 343–57. http://dx.doi.org/10.30574/wjarr.2024.23.2.2349.

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The Aβ peptide, which is connected to the development of Alzheimer's disease, forms highly neurotoxic prefibrillar oligomeric aggregates, which are challenging to study due to their fleeting, low prevalence, and diverse nature. These aggregates are considered to play a role in the pathogenesis of numerous neurodegenerative diseases. The potential approach of blocking or disrupting the buildup of amyloid peptides, particularly amyloid-β (AβOs), by using nanoparticles that specifically bind or prevent their aggregation to develop new medications and treatments for Alzheimer's disease (AD) could

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7

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 (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

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8

Agaeva, G., and G. Najafova. "ELECTRONIC PARAMETERS OF CONFORMATIONAL STATES OF ABETA-AMYLOID PEPTIDE (25-35)." Russian Journal of Biological Physics and Chemisrty 8, no. 1 (2024): 21–26. http://dx.doi.org/10.29039/rusjbpc.2023.0583.

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The electronic characteristics of stable conformational states of beta-amyloid peptide (25-35) have been studied by molecular modeling methods. Beta-amyloid peptide (Aβ) is the main component of senile plaques found in the brains of patients with Alzheimer's disease. Aβ (25-35) fragment of a molecule with the amino acid sequence Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met. It has been shown that the conformational features of a molecule are largely determined by its environment; therefore, the aim of this work was to study the differences in the conformations of amyloid beta-peptide (25-35) in

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9

Jensen, P. H., E. S. Sørensen, T. E. Petersen, J. Gliemann та L. K. Rasmussen. "Residues in the synuclein consensus motif of the α-synuclein fragment, NAC, participate in transglutaminase-catalysed cross-linking to Alzheimer-disease amyloid βA4 peptide". Biochemical Journal 310, № 1 (1995): 91–94. http://dx.doi.org/10.1042/bj3100091.

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The widespread deposition of amyloid plaques is one of the hallmarks of Alzheimer disease (AD). A recently described component of amyloid plaques is the 35-residue peptide, non-A beta component of AD amyloid, which is derived from a larger intracellular neuronal constituent, alpha-synuclein. We demonstrate that transglutaminase catalyses the formation of the covalent non-A beta component of AD amyloid polymers in vitro as well as polymers with beta-amyloid peptide, the major constituent of AD plaques. The transglutaminase-reactive amino acid residues in the non-A beta component of AD amyloid w

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10

Ghiso, J., E. Matsubara, A. Koudinov та ін. "The cerebrospinal-fluid soluble form of Alzheimer's amyloid β is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex". Biochemical Journal 293, № 1 (1993): 27–30. http://dx.doi.org/10.1042/bj2930027.

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The amyloid fibrils deposited in Alzheimer's neuritic plaque cores and cerebral blood vessels are mainly composed of aggregated forms of a unique peptide, 39-42 amino acids long, named amyloid beta (A beta). A similar, although soluble, A beta (‘sA beta’) has been identified in cerebrospinal fluid, plasma and cell supernatants, indicating that it is normally produced by proteolytic processing of its precursor protein, amyloid precursor protein (APP). Using direct binding experiments we have isolated and characterized an 80 kDa circulating protein that specifically interacts with a synthetic pe

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Naushad, Mehjabeen, Siva Sundara Kumar Durairajan, Amal Kanti Bera, Sanjib Senapati та Min Li. "Natural Compounds with Anti-BACE1 Activity as Promising Therapeutic Drugs for Treating Alzheimerʼs Disease". Planta Medica 85, № 17 (2019): 1316–25. http://dx.doi.org/10.1055/a-1019-9819.

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AbstractAlzheimerʼs disease is a neurodegenerative disease that leads to irreversible neuronal damage. Senile plaques, composed of amyloid beta peptide, is the principal abnormal characteristic of the disease. Among the factors involved, the secretase enzymes, namely, α secretase, beta-site amyloid precursor protein-cleaving enzyme, β secretase, and γ secretase, hold consequential importance. Beta-site amyloid precursor protein-cleaving enzyme 1 is considered to be the rate-limiting factor in the production of amyloid beta peptide. Research supporting the concept of inhibition of beta-site amy

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12

Mousavi, ayed Yousof, and Aqdas Bayat. "Alzheimer's Disease and the Beta Amyloid: A review of animal studies." Scientific-Research Quarterly Journal of Medical Science 9, no. 18 (2025): 1–10. https://doi.org/10.62134/kjms09181.

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Introduction: Loss of ability to perform daily activities, impairment of cognition and memory impairments are the clinical symptoms of Alzheimer's disease (the most common form of dementia). There are two neuropathological signs for diagnosis of Alzheimer's disease: 1. extracellular deposition of peptide A; 2. accumulation of phosphorylated tau in neurofibrillary tangles in neurons. Beta Amyloid that originally called A4 amyloid protein, is one of the most important insoluble brain peptides studied in neuroscience. Methods: The data of this study were collected from original and scientific art

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13

Usui, Kenji, Shin-ichiro Yokota, Kazuya Iwata, and Yoshio Hamada. "Novel Purification Process for Amyloid Beta Peptide(1-40)." Processes 8, no. 4 (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, purif

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Barden, C., F. Meier-Stephenson, MD Carter, 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 (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

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15

Airoldi, Cristina, Francisco Cardona, Erika Sironi, et al. "Fluorescent amyloid β-peptide ligand derivatives as potential diagnostic tools for Alzheimer’s disease." Pure and Applied Chemistry 85, no. 9 (2013): 1813–23. http://dx.doi.org/10.1351/pac-con-12-11-07.

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A&beta;-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 &beta;-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&ndash;brain barrier (BBB) and to stain A&beta;‑deposits.

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16

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 (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 co

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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 (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 mo

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18

Borutaite, Vilmante, Ramune Morkuniene, and Gintaras Valincius. "Beta-amyloid oligomers: recent developments." BioMolecular Concepts 2, no. 3 (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

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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 (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

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Haass, C., E. H. Koo, A. Capell, D. B. Teplow, and D. J. Selkoe. "Polarized sorting of beta-amyloid precursor protein and its proteolytic products in MDCK cells is regulated by two independent signals." Journal of Cell Biology 128, no. 4 (1995): 537–47. http://dx.doi.org/10.1083/jcb.128.4.537.

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Progressive cerebral deposition of the amyloid (A beta) beta-protein is an early and invariant feature of Alzheimer's disease. A beta is derived by proteolysis from the membrane-spanning beta-amyloid precursor protein (beta APP). beta APP is processed into various secreted products, including soluble beta APP (APPs), the 4-kD A beta peptide, and a related 3-kD peptide (p3). We analyzed the mechanisms regulating the polarized basolateral sorting of beta APP and its proteolytic derivatives in MDCK cells. Deletion of the last 32 amino acids (residues 664-695) of the beta APP cytoplasmic tail had

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Festa, Giulia, Francesco Mallamace, Giulia Maria Sancesario 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 (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

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22

Matos, Jason O., Greg Goldblatt, and Suren A. Tatulian. "Pyroglutamylated Amyloid-Beta Peptide Reverses Cross Beta-Sheets by a Prion-Like Mechanism." Biophysical Journal 106, no. 2 (2014): 684a—685a. http://dx.doi.org/10.1016/j.bpj.2013.11.3788.

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23

Gera, János, and Gábor Paragi. "Fluorescence-Labeled Amyloid Beta Monomer: A Molecular Dynamical Study." Molecules 25, no. 15 (2020): 3524. http://dx.doi.org/10.3390/molecules25153524.

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The aggregation process of the Amyloidβ (Aβ) peptide is one of the central questions in Alzheimers’s research. Fluorescence-labeled single-molecule detection is a novel technique concerning the early stage investigation of Aβ aggregation, where the labeling dyes are covalently bound to the Aβ monomer. As the influence of the dye on the conformational space of the Aβ monomer can be significant, its effect on the seeding process is an open question. The applied fluorescent molecule continuously switches between an active (ON) and an inactive (OFF) state, where the latter supports an extra rotati

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Candreva, Jason, Edward Chau, Edwin Aoraha, Vikas Nanda та Jin Ryoun Kim. "Hetero-assembly of a dual β-amyloid variant peptide system". Chemical Communications 54, № 49 (2018): 6380–83. http://dx.doi.org/10.1039/c8cc02724b.

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Nguyen, Ngoc Kim, Bella Poduska, Mia Franks, et al. "A Copper-Selective Sensor and Its Inhibition of Copper-Amyloid Beta Aggregation." Biosensors 14, no. 5 (2024): 247. http://dx.doi.org/10.3390/bios14050247.

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Copper is an essential trace metal for biological processes in humans and animals. A low level of copper detection at physiological pH using fluorescent probes is very important for in vitro applications, such as the detection of copper in water or urine, and in vivo applications, such as tracking the dynamic copper concentrations inside cells. Copper homeostasis is disrupted in neurological diseases like Alzheimer’s disease, and copper forms aggregates with amyloid beta (Ab42) peptide, resulting in senile plaques in Alzheimer’s brains. Therefore, a selective copper detector probe that can det

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Eckenhoff, Roderic G., Jonas S. Johansson, Huafeng Wei та ін. "Inhaled Anesthetic Enhancement of Amyloid-β Oligomerization and Cytotoxicity". Anesthesiology 101, № 3 (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

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JALILI, S., та M. AKHAVAN. "A MOLECULAR DYNAMICS SIMULATION STUDY OF CONFORMATIONAL CHANGES AND SOLVATION OF Aβ PEPTIDE IN TRIFLUOROETHANOL AND WATER". Journal of Theoretical and Computational Chemistry 08, № 02 (2009): 215–31. http://dx.doi.org/10.1142/s0219633609004769.

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Molecular dynamics (MD) simulations of amyloid beta peptide have been performed in aqueous solutions of trifluoroethanol with different concentrations. The amount of α-helical secondary structure increases when going from pure water to trifluoroethanol-rich solutions. The conformation obtained in 40% (v/v) trifluoroethanol solution is very similar to the experimental observations of beta peptide in sodium dodecyl sulfate micelle. In this solution, the peptide has two helical segments connected through a looped region. The C-terminal helix of beta peptide unfolds in pure water. The effect of tr

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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 (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 st

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Gomes, Luiza M. F., Atif Mahammed, Kathleen E. Prosser, et al. "A catalytic antioxidant for limiting amyloid-beta peptide aggregation and reactive oxygen species generation." Chemical Science 10, no. 6 (2019): 1634–43. http://dx.doi.org/10.1039/c8sc04660c.

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Paulsson, Johan F., Sebastian W. Schultz, Martin Köhler, Ingo Leibiger, Per-Olof Berggren, and Gunilla T. Westermark. "Real-Time Monitoring of Apoptosis by Caspase-3-Like Protease Induced FRET Reduction Triggered by Amyloid Aggregation." Experimental Diabetes Research 2008 (2008): 1–12. http://dx.doi.org/10.1155/2008/865850.

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Amyloid formation is cytotoxic and can activate the caspase cascade. Here, we monitor caspase-3-like activity as reduction of fluorescence resonance energy transfer (FRET) using the contstruct pFRET2-DEVD containing enhanced cyan fluorescent protin (EYFP) linked by the caspase-3 specific cleavage site residues DEVD. Beta-TC-6 cells were transfected, and the fluoorescence was measured at 440 nm excitation and 535 nm (EYFP) and 480 nm (ECFP) emission wavelength. Cells were incubated with recombinant pro lset Amyloid Polypeptide (recprolAPP) or the processing metabolites of prolAPP; the N-termina

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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 (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 for

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Ramaswamy, Keerthana, Priyadharshini Kumaraswamy, Swaminathan Sethuraman, and Uma Maheswari Krishnan. "Self-assembly characteristics of a structural analogue of Tjernberg peptide." RSC Adv. 4, no. 32 (2014): 16517–23. http://dx.doi.org/10.1039/c3ra47754a.

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This article aims to understand the pathogenesis behind the formation of amyloid plaques using a modified version of the KLVFF peptide. It was found that the cytotoxicity of the nanostructures formed by the RIVFF peptide may be attributed to the aminoacids with long side chains along with hydrophobic aminoacids resembling the amyloid beta peptide.

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Lange, Johannes, Kristin Aaser Lunde, Camilla Sletten, et al. "Association of aBACE1Gene Polymorphism with Parkinson’s Disease in a Norwegian Population." Parkinson's Disease 2015 (2015): 1–5. http://dx.doi.org/10.1155/2015/973298.

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Background. Parkinson’s disease (PD) and Alzheimer’s disease (AD) share pathological features, including amyloid-beta pathology. Amyloid-beta peptide is generated by sequential proteolysis of amyloid precursor protein (APP), and genetic variations in the processing pathway genes have been found to increase the risk of AD; however, the contribution in PD is unknown.Methods. The aim of this study was to investigate whether candidate polymorphisms in five genes (ADAM10,BACE1,BACE2,PSEN2, andCLU) involved in the APP processing pathway affect PD risk in a population-based cohort of patients with in

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Schreiner, Thomas Gabriel, Oliver Daniel Schreiner, Maricel Adam, and Bogdan Ovidiu Popescu. "The Roles of the Amyloid Beta Monomers in Physiological and Pathological Conditions." Biomedicines 11, no. 5 (2023): 1411. http://dx.doi.org/10.3390/biomedicines11051411.

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Amyloid beta peptide is an important biomarker in Alzheimer’s disease, with the amyloidogenic hypothesis as one of the central hypotheses trying to explain this type of dementia. Despite numerous studies, the etiology of Alzheimer’s disease remains incompletely known, as the pathological accumulation of amyloid beta aggregates cannot fully explain the complex clinical picture of the disease. Or, for the development of effective therapies, it is mandatory to understand the roles of amyloid beta at the brain level, from its initial monomeric stage prior to aggregation in the form of senile plaqu

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Kellermayer, Miklós SZ, Ünige Murvai, Andrea Horváth, Emöke Lászlóffi, Katalin Soós та Botond Penke. "Epitaxial assembly dynamics of mutant amyloid β25–35_N27C ﬁbrils explored with time-resolved scanning force microscopy". Biophys Chem. 184C (5 вересня 2013): 54–61. https://doi.org/10.1016/j.bpc.2013.08.007.

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Amyloid β25–35 (Aβ25–35) is a toxic fragment of Alzheimer's beta peptide. We have previously shown that Aβ25–35 fibrils form a trigonally oriented network on mica by epitaxial growth mechanisms. Chemical reactivity can be furnished to the fibril by introducing a cysteine residue (Aβ25–35_N27C) while maintaining oriented assembly properties. Previously we have shown that fibril binding to mica is strongly influenced by KCl concentration. In the present work we explored the kinetics of epitaxial assembly of the mutant fibrils at different peptide a

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Datki, Zsolt, Rita Sinka, Brian J. Dingmann, et al. "Protective Effect of a Hexapeptide Derived from Rotifer-Specific SCO-Spondin Against Beta-Amyloid Toxicity." International Journal of Molecular Sciences 26, no. 11 (2025): 5109. https://doi.org/10.3390/ijms26115109.

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The Rotimer (rotifer-specific biopolymer) like SCO-spondin (R-SSPO/1), predicted as the main component of this biopolymer, is an adequate base for the design of functional small peptides. This macromolecule is interactive and protective against neurotoxic human-type beta-amyloid 1-42 aggregates (agg-Aβ). The current work presents biological investigations and predictable molecular interaction analysis of DSSNDL and PNCRDGSDE peptides that were synthesized based on the sequences of R-SSPO/1. Viability assays (NADH-dependent cellular reduction capacity, intracellular esterase activity, and motil

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Mattson, M. P. "Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives." Physiological Reviews 77, no. 4 (1997): 1081–132. http://dx.doi.org/10.1152/physrev.1997.77.4.1081.

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beta-Amyloid precursor protein (beta-APP), the source of the fibrillogenic amyloid beta-peptide (A beta) that accumulates in the brain of victims of Alzheimer's disease, is a multifunctional protein that is widely expressed in the nervous system. beta-Amyloid precursor protein is axonally transported and accumulates in presynaptic terminals and growth cones. A secreted form of beta-APP (sAPP alpha) is released from neurons in response to electrical activity and may function in modulation of neuronal excitability, synaptic plasticity, neurite outgrowth, synaptogenesis, and cell survival. A sign

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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 (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 neuroprote

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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 (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 fo

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Makino, Mitsuhiro, Kaori Ito-Takahashi, Akira Yano, et al. "P2-395: Effect of a novel beta-amyloid peptide vaccine on brain beta-amyloid deposition in Tg2576 mice." Alzheimer's & Dementia 9 (July 2013): P502—P503. http://dx.doi.org/10.1016/j.jalz.2013.05.1044.

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Wirths, Oliver, Gerd Multhaup, and Thomas A. Bayer. "A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide - the first step of a fatal cascade." Journal of Neurochemistry 91, no. 3 (2004): 513–20. http://dx.doi.org/10.1111/j.1471-4159.2004.02737.x.

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Strosznajder, J. B., H. Jeśko, and R. P. Strosznajder. "Effect of amyloid beta peptide on poly(ADP-ribose) polymerase activity in adult and aged rat hippocampus." Acta Biochimica Polonica 47, no. 3 (2000): 847–54. http://dx.doi.org/10.18388/abp.2000_4003.

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It is suggested that the fibrillar amyloid beta peptide (A beta) in brain plays a direct role in neurodegeneration in Alzheimer's disease, probably through activation of reactive oxygen species formation. Free radicals and numerous neurotoxins elicit DNA damage that subsequently activates poly(ADP-ribose) polymerase (PARP, EC 2.4.2.30). In this study the effect of neurotoxic fragment (25-35) of full length A beta peptide on PARP activity in adult and aged rat hippocampus was investigated. In adult (4 month old) rat hippocampus the A beta 25-35 peptide significantly enhanced PARP activity by ab

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Owens, Lauren, Joshua Bracewell, Alexandre Benedetto, Neil Dawson, Christopher Gaffney та Edward Parkin. "BACE1 Overexpression Reduces SH-SY5Y Cell Viability Through a Mechanism Distinct from Amyloid-β Peptide Accumulation: Beta Prime-Mediated Competitive Depletion of sAβPPα". Journal of Alzheimer's Disease 86, № 3 (2022): 1201–20. http://dx.doi.org/10.3233/jad-215457.

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Background: The Alzheimer’s disease (AD)-associated amyloid-beta protein precursor (AβPP) can be cleaved by β-site AβPP cleaving enzyme 1 (BACE1) and the γ-secretase complex to yield neurotoxic amyloid-β (Aβ) peptides. However, AβPP can also be cleaved in a ‘non-amyloidogenic’ manner either by α-secretase to produce soluble AβPP alpha (sAβPPα) (a fragment with neuroprotective/neurogenic functions) or through alternative BACE1-mediated ‘beta prime’ activity yielding soluble AβPP beta prime (sAβPPβ’). Objective: To determine whether sAβPPα depletion, as opposed to Aβ peptide accumulation, contri

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Ghiso, J., A. Rostagno, J. E. Gardella, L. Liem, P. D. Gorevic, and B. Frangione. "A 109-amino-acid C-terminal fragment of Alzheimer's-disease amyloid precursor protein contains a sequence, -RHDS-, that promotes cell adhesion." Biochemical Journal 288, no. 3 (1992): 1053–59. http://dx.doi.org/10.1042/bj2881053.

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Amyloid beta (A beta), the major constituent of the fibrils composing senile plaques and vascular amyloid deposits in Alzheimer's disease (AD) and related disorders, is a 39-42-residue self-aggregating degradation peptide of a larger multidomain membrane glycoprotein designated amyloid precursor protein (APP). An array of biological functions has been assigned to different APP domains, including growth regulation, neurotoxicity, inhibitory activity of serine proteinases and promotion of cell-cell and cell-matrix interactions. A beta is generated through an as-yet-unknown catabolic pathway that

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Lugovskaya, Elizaveta, Giulia Codagnone, Ivan Sanavia, et al. "Search for potential Alzheimer’s disease therapeutics: Identification of inhibitors of amyloid oligomerization with high affinity for the zinc-binding site." Journal of Multiscale Neuroscience 3, no. 3 (2024): 186–99. http://dx.doi.org/10.56280/1641424663.

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The progression of Aβ peptide aggregation in the brain has been suggested to play a significant role in the pathogenesis and development of Alzheimer’s disease. This study is intended to provide insight into the interactions between the zinc-binding site of beta-amyloids and the zinc ion itself. The absence of zinc bonded to the beta-amyloid has been shown to potentially slow down the progression of Alzheimer's disease, so the goal is to provide an analysis of available drugs that can be repurposed and could profoundly impact Alzheimer's disease treatment. We address how and with what strength

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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 (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 an

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Zaretsky, Dmitry V., Maria V. Zaretskaia, and Yaroslav I. Molkov. "Patients with Alzheimer’s disease have an increased removal rate of soluble beta-amyloid-42." PLOS ONE 17, no. 10 (2022): e0276933. http://dx.doi.org/10.1371/journal.pone.0276933.

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Senile plaques, which are mostly composed of beta-amyloid peptide, are the main signature of Alzheimer’s disease (AD). Two main forms of beta-amyloid in humans are 40 and 42-amino acid, long; the latter is considered more relevant to AD etiology. The concentration of soluble beta-amyloid-42 (Aβ42) in cerebrospinal fluid (CSF-Aβ42) and the density of amyloid depositions have a strong negative correlation. However, AD patients have lower CSF-Aβ42 levels compared to individuals with normal cognition (NC), even after accounting for this correlation. The goal of this study was to infer deviations o

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Chandrol, Sweta, Sandeep Gupta, and Prashant Tiwari. "Recent Progress in Alzheimer’s Disease: Pathophysiology, Newer Natural & Synthetic Inhibitors, and Therapeutic Targets." International Journal of Medical & Pharmaceutical Sciences 14, no. 01 (2024): 07–14. http://dx.doi.org/10.31782/ijmps.2024.14102.

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The inability to remember recent events, process new information, or complete even the most basic of tasks is a hallmark of Alzheimer’s disease, an irreversible neurodegenerative brain illness. Among those 65 and older, it is the leading cause of dementia. When a person’s cognitive and behavioural skills deteriorate to the point that they become a burden in everyday life, we say that they have dementia.There is currently no known way to halt the progression of AD or stop its symptoms from occurring. Huge literature survey was conducted from various popular medical databases such as Google Scho

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TAKENOUCHI, Takahito, and Eisuke MUNEKATA. "Amyloid .BETA.-Peptide. A Putative Key Substance of Alzheimer's Disease." Kagaku To Seibutsu 33, no. 12 (1995): 776–83. http://dx.doi.org/10.1271/kagakutoseibutsu1962.33.776.

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Hu, Yang, Baihao Su, HeQiu Zheng, and Jin Ryoun Kim. "A peptide probe for detection of various beta-amyloid oligomers." Molecular BioSystems 8, no. 10 (2012): 2741. http://dx.doi.org/10.1039/c2mb25148e.

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