Готові списки джерел за темами / Beta-Amyloid peptides

Добірка наукової літератури з теми "Beta-Amyloid peptides"

Автор: Grafiati

Опубліковано: 7 липня 2024

Оновлено: 7 липня 2024

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Статті в журналах з теми "Beta-Amyloid peptides":

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

Більше джерел

Дисертації з теми "Beta-Amyloid peptides":

Kadlčík, Vojtěch. "Oxidation of beta-amyloid and model peptides." Paris 11, 2006. http://www.theses.fr/2006PA112008.

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Le but de mon travail de thèse était de caractériser les produits de l'oxydation du peptide beta-amyloïde (Abeta) impliqué dans le développement de la maladie d'Alzheimer. Pour étudier l'effet de la structure de peptide sur les processus redox, les propriétés du peptide Abeta (1-40) ont été comparées au peptide de séquence inverse, Abeta (40-1). Les radicaux libres choisis ont été produits en radiolyse gamma. Les produits finaux ont été caractérisés par des techniques d'analyse diverses (HPLC, GC, MALDI-TOF MS, spectrométrie de fluorescence, spectrométrie raman). Pour établir l'effet de l'environnement sur le processus d'oxydation, peptides ont été oxydés dans trois systèmes différents: solution aqueuse homogène, milieu micellaire (SDS) et système des vésicules phospholipidiques (POPC). En solution aqueuse homogène, les produits d'oxydation sont différents pour les deux peptides. Les résidus facilement oxydables sont Met35 pour Abeta(1-40) et Tyr10 pour Abeta(40-1). La présence des micelles ainsi que des vésicules phospholipidiques change profondément le cours de l'oxydation. Une étude structurale en dichroïsme circulaire nous permet d'avancer des hypothèses pour interpréter ces résultats. Nous avons montré que des produits de dégradation des peptides Abeta peuvent induire d'une manière catalytique l'altération des phospholipides. Cette propriété est attribuée à l'action des atomes d'hydrogène sur le peptide. Nos résultats sont intéressants dans le contexte du développement de la maladie d'Alzheimer, car ils peuvent aider à éclairer le rôle de l'interaction de peptide Abeta(1-40) avec des membranes phospholipidique dans les propriétés redox du peptide
The goal of my thesis work was to characterize oxidation products of beta-amyloid peptide (Abeta), which is implied in the development of Alzheimer's disease. To study the effect of peptide structure on the redox processes, oxidation properties of Abeta(1-40) were compared to the peptide with reverse sequence, Abeta(40-1). Azide and hydroxyl radicals used for oxidation were produced by gamma radiolysis. Final products were characterized by a variety of analytical techniques (HPLC, GC, MALDI-TOF MS, fluorescence and raman spectrometry). To establish the role of peptide environment on its redox properties, oxidation was carried out in three different systems: homogeneous aqueous solution, micellar system (SDS) and in the presence of phospholipids vesicles (POPC). In homogeneous aqueous solution, oxidation products are different for both peptides. The main oxidation targets are Met35 for Abeta(1-40) and Tyr10 for Abeta(40-1). The presence of micelles and phospholipid vesicles has an important impact on the oxidation pathways. These changes could be related to changes in peptide conformations studied by circular dichroism. We have also shown that Abeta degradation products may catalytically induce alternation of phospholipids. This process is initiated by reaction of hydrogen radicals with the peptide. Our results are interesting in the context of the development of Alzheimer's disease as they may bring an insight into the role of Abeta(1-40) interaction with phospholipids membrane for the redox properties of the peptide

Tanase, Maria Elena. "Nanomaterials self-assembly driven by beta-amyloid peptides." ScholarWorks@UNO, 2005. http://louisdl.louislibraries.org/u?/NOD,223.

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Thesis (M.S.)--University of New Orleans, 2005.
Title from electronic submission form. "A thesis ... in partial fulfillment of the requirements for the degree of Master of Science in the Department of Chemistry"--Thesis t.p. Vita. Includes bibliographical references.

Chen, Zhongjing. "NMR structural characterization of beta-amyloid peptides and their inhibitors." [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=973392266.

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Kittner, Madeleine. "Folding and aggregation of amyloid peptides." Phd thesis, Universität Potsdam, 2011. http://opus.kobv.de/ubp/volltexte/2011/5357/.

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Aggregation of the Amyloid β (Aβ) peptide to amyloid fibrils is associated with the outbreak of Alzheimer’s disease. Early aggregation intermediates in form of soluble oligomers are of special interest as they are believed to be the major toxic components in the process. These oligomers are of disordered and transient nature. Therefore, their detailed molecular structure is difficult to access experimentally and often remains unknown. In the present work extensive, fully atomistic replica exchange molecular dynamics simulations were performed to study the preaggregated, monomer states and early aggregation intermediates (dimers, trimers) of Aβ(25-35) and Aβ(10-35)-NH2 in aqueous solution. The folding and aggregation of Aβ(25-35) were studied at neutral pH and 293 K. Aβ(25-35) monomers mainly adopt β-hairpin conformations characterized by a β-turn formed by residues G29 and A30, and a β-sheet between residues N27–K28 and I31–I32 in equilibrium with coiled conformations. The β-hairpin conformations served as initial configurations to model spontaneous aggregation of Aβ(25-35). As expected, within the Aβ(25-35) dimer and trimer ensembles many different poorly populated conformations appear. Nevertheless, we were able to distinguish between disordered and fibril-like oligomers. Whereas disordered oligomers are rather compact with few intermolecular hydrogen bonds (HBs), fibril-like oligomers are characterized by the formation of large intermolecular β-sheets. In most of the fibril-like dimers and trimers individual peptides are fully extended forming in- or out-of-register antiparallel β-sheets. A small amount of fibril-like trimers contained V-shaped peptides forming parallel β-sheets. The dimensions of extended and V-shaped oligomers correspond well to the diameters of two distinct morphologies found for Aβ(25-35) fibrils. The transition from disordered to fibril-like Aβ(25-35) dimers is unfavorable but driven by energy. The lower energy of fibril-like dimers arises from favorable intermolecular HBs and other electrostatic interactions which compete with a loss in entropy. Approximately 25 % of the entropic cost correspond to configurational entropy. The rest relates to solvent entropy, presumably caused by hydrophobic and electrostatic effects. In contrast to the transition towards fibril-like dimers the first step of aggregation is driven by entropy. Here, we compared structural and thermodynamic properties of the individual monomer, dimer and trimer ensembles to gain qualitative information about the aggregation process. The β-hairpin conformation observed for monomers is successively dissolved in dimer and trimer ensembles while instead intermolecular β-sheets are formed. As expected upon aggregation the configurational entropy decreases. Additionally, the solvent accessible surface area (SASA), especially the hydrophobic SASA, decreases yielding a favorable solvation free energy which overcompensates the loss in configurational entropy. In summary, the hydrophobic effect, possibly combined with electrostatic effects, yields an increase in solvent entropy which is believed to be one major driving force towards aggregation. Spontaneous folding of the Aβ(10-35)-NH2 monomer was modeled using two force fields, GROMOS96 43a1 and OPLS/AA, and compared to primary NMR data collected at pH 5.6 and 283 K taken from the literature. Unexpectedly, the two force fields yielded significantly different main conformations. Comparison between experimental and calculated nuclear Overhauser effect (NOE) distances is not sufficient to distinguish between the different force fields. Additionally, the comparison with scalar coupling constants suggest that the chosen protonation in both simulations corresponds to a pH lower than in the experiment. Based on this analysis we were unable to determine which force field yields a better description of this system. Dimerization of Aβ(10-35)-NH2 was studied at neutral pH and 300 K. Dimer conformations arrange in many distinct, poorly populated and rather complex alignments or interlocking patterns which are rather stabilized by side chain interactions than by specific intermolecular hydrogen bonds. Similar to Aβ(25-35) dimers, transition towards β-sheet-rich, fibril-like Aβ(10-35) dimers is driven by energy competing with a loss in entropy. Here, transition is mediated by favorable peptide-solvent and solvent-solvent interactions mainly arising from electrostatic interactions.
Die Aggregation des Amyloid β (Aβ) Peptids zu Amyloidfibrillen wird mit dem Ausbruch der Alzheimer Krankheit in Verbindung gebracht. Die toxische Wirkung auf Zellen wird vor allem den zeitigen Intermediaten in Form von löslichen Oligomeren zugeschrieben. Aufgrund deren ungeordneter und flüchtiger Natur kann die molekulare Struktur solcher zeitigen Oligomere oft experimentell nicht aufgelöst werden. In der vorliegenden Arbeit wurden aufwendige atomistische Replica-Exchange-Molekulardynamik-Simulationen durchgeführt, um die molekulare Struktur von Monomeren und Oligomeren der Fragmente Aβ(25-35) und Aβ(10-35)-NH2 in Wasser zu untersuchen. Die Faltung und Aggregation von Aβ(25-35) wurde bei neutralem pH und 293 K untersucht. Monomere dieses Fragments bilden hauptsächlich β-Haarnadelkonformationen im Gleichgewicht mit Knäulstrukturen. Innerhalb der β-Haarnadelkonformationen bilden die Residuen G29 und A30 einen β-turn, während N27–K28 and I31–I32 ein β-Faltblatt bilden. Diese β-Haarnadelkonformationen bildeten den Ausgangspunkt zur Modellierung spontaner Aggregation. Wie zu erwarten, bilden sich eine Vielzahl verschiedener, gering besetzter Dimer- und Trimerkonformationen. Mit Hilfe einer gröberen Einteilung können diese in ungeordnete und fibrillähnliche Oligomere unterteilt werden. Ungeordnete Oligomere bilden kompakte Strukturen, die nur durch wenige intermolekulare Wasserstoffbrückenbindungen (HBB) stabilisiert sind. Typisch für fibrillähnliche Oligomere ist hingegen die Ausbildung großer intermolekularer β-Faltblätter. In vielen dieser Oligomere finden wir antiparallele, in- oder out-of-register β-Faltblätter gebildet durch vollständig ausgestreckte Peptide. Ein kleiner Teil der fibrillähnlichen Trimere bildet parallele, V-förmige β-Faltblätter. Die Ausdehnungen ausgestreckter und V-förmiger Oligomere entspricht in etwa den Durchmessern von zwei verschiedenen, experimentell gefundenen Fibrillmorphologien für Aβ(25-35). Die Umwandlung von ungeordneten zu fibrillähnlichen Aβ(25-35) Dimeren ist energetisch begünstigt, läuft aber nicht freiwillig ab. Fibrillähnliche Dimere haben eine geringere Energie aufgrund günstiger Peptidwechselwirkungen (HBB, Salzbrücken), welche durch den Verlust an Entropie kompensiert wird. Etwa 25 % entsprechen dem Verlust an Konfigurationsentropie. Der restliche Anteil wird einem Verlust an Lösungsmittelentropie aufgrund von hydrophoben und elektrostatischen Effekten zugesprochen. Im Gegensatz zur Umwandlung in fibrillähnliche Dimere, ist die Assoziation von Monomeren oder Oligomeren entropisch begünstigt. Beim Vergleich thermodynamischer Eigenschaften der Monomer-, Dimer- und Trimersysteme zeigt sich im Verlauf der Aggregation, wie erwartet, eine Abnahme der Konfigurationsentropie. Zusätzlich nimmt die dem Lösungsmittel zugängliche Oberfläche (SASA), insbesondere die hydrophobe SASA, ab. In Verbindung damit beobachten wir eine Abnahme der freien Solvatisierungsenergie, welche den Verlust an Konfigurationsentropie kompensiert. Mit anderen Worten, der hydrophobe Effekt in Kombination mit elektrostatischen Wechselwirkungen führt zu einem Ansteigen der Lösungsmittelentropie und begünstigt damit die Aggegation. Die spontane Faltung des Aβ(10-35)-NH2 Monomers wurde für zwei verschiedene Proteinkraftfelder, GROMOS96 43a1 und OPLS/AA, untersucht und mit primären NMR-Daten aus der Literatur, gemessen bei pH 5.6 und 283 K, verglichen. Beide Kraftfelder generieren unterschiedliche Hauptkonformationen. Der Vergleich zwischen experimentellen und berechneten Kern-Overhauser-Effekt (NOE) Abständen ist nicht ausreichend, um zwischen beiden Kraftfeldern zu unterscheiden. Der Vergleich mit Kopplungskonstanten aus Experiment und Simulation zeigt, dass beide Simulationen einem pH-Wert geringer als 5.6 ensprechen. Basierend auf den bisherigen Ergebnissen können wir nicht entscheiden, welches Kraftfeld eine bessere Beschreibung für dieses System liefert. Die Dimerisierung von Aβ(10-35)-NH2 wurde bei neutralem pH und 300 K untersucht. Wir finden eine Vielzahl verschiedener, gering besetzter Dimerstrukturen, welche eher durch Seitenkettenkontakte als durch spezifische HBB stabilisiert sind. Wie bei den Aβ(25-35) Dimeren, ist die Umwandlung zu β-Faltblattreichen, fibrillähnlichen Aβ(10-35) Dimeren energetisch begünstigt, konkurriert aber mit einem Entropieverlust. Die Umwandlung wird in diesem Fall durch elektrostatische Wechselwirkungen zwischen Peptid und Lösungsmittel und innerhalb des Lösungsmittels bestimmt.

Davison, Catherine J. "The interactions of the C-terminus of acetlycholinesterase with amyloid-beta peptides." Thesis, University of Oxford, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.496845.

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Tang, Christian C. "Structure and Activity of Metallo-Peptides." Scholar Commons, 2017. http://scholarcommons.usf.edu/etd/6961.

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Metal ions are ubiquitously found in all living systems and play vital roles in supporting life forms by performing an array of biological activities. Such biological activities include binding and transforming organic molecules, and also acting as active centers and cofactors for catalysis of various acid-base and redox reactions in biological system. The main focus in bioinorganic chemistry is to elucidate the structural and functional roles of metals in biological systems. Among all transition metal ions, Cu2+ and Fe3+ are especially versatile and important due to their abilities to go through redox efficiently. This dissertation can be divided into four main chapters. The bioinorganic chemistry of Cu- and Fe-containing proteins were briefly discussed in Chapter one. The next chapter focuses on bacitracin, a cyclic peptide-based antibiotic produced by soil bacteria Bacillus subtilis. Bacitracin is a metalloantibiotics that can coordinate with many transition metal ions and exhibit different biological activities. In the first part of Chapter two, the aim is to explore the chemicals interactions in soil micro-ecology by investigating the interactions of different flavonoids and Cu(II)-bacitracin complex. The second part of chapter two demonstrated the binding and oxidation activity of iron(III)-bacitracin. Metal-mediated oxidative stress plays a crucial role in the development of different neurodegenerative diseases. In chapter 3, various synthetic and natural compounds were used to inhibit the oxidation chemistry mediated by Cu(II)-beta-amyloid complex associated with Alzheimer’s disease. Many proteins incorporate copper ions at their active sites for different functions, and among all of the chemistry copper-containing-proteins can perform, one of the most interesting aspect is the ability to bind and activate O2. Therefore, the biomimetic of two different Cu(II) complexes were investigated. In all studies, a combination of kinetic and different spectroscopic methods (UV-vis, NMR and resonance Raman spectroscopy) were used to study their metal binding and activity.

Mishra, Pamela Haradhan. "Unbinding of abeta peptides from amyloid fibrils explicit solvent molecular dynamics study /." Fairfax, VA : George Mason University, 2008. http://hdl.handle.net/1920/3419.

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Thesis (M.S.)--George Mason University, 2008.
Vita: p. 48. Thesis director: Dmitri Klimov. Submitted in partial fulfillment of the requirements for the degree of Master of Science in Bioinformatics and Computational Biology. Title from PDF t.p. (viewed Mar. 17, 2009). Includes bibliographical references (p. 45-47). Also issued in print.

Mikkonen, Saara. "Electrophoretic focusing in microchannels combined with mass spectrometry : Applications on amyloid beta peptides." Doctoral thesis, KTH, Tillämpad fysikalisk kemi, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-193134.

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Analysis of low-abundance components in small samples remains a challenge within bioanalytical chemistry, and new techniques for sample pretreatments followed by sensitive and informative detection are required. In this thesis, procedures for preconcentration and separation of proteins and peptides in open microchannels fabricated on silicon microchips are presented. Analyte electromigration was induced by applying a voltage along the channel length, and detection was performed either by matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) within the open channel, or by sampling a nL fraction containing the preconcentrated analytes from the channel for subsequent nano-electrospray ionization- (nESI-) or MALDI-MS. Utilizing solvent evaporation from the open system during sample supply, sample volumes exceeding the 25-75 nL channel volume could be analyzed. For preconcentration/separation of components in the discrete channel volume a lid of inert fluorocarbon liquid was used for evaporation control. In Papers I and II, aqueous, carrier-free solutions of proteins and peptides were analyzed, and the method was successfully applied for fast and simple preconcentration of amyloid beta (Aβ) peptides, related to Alzheimer’s disease. The impact of possible impurities in the analysis of carrier-free solutions was investigated in Paper III with the 1D simulation software GENTRANS, and a method for open-channel isoelectric focusing in a tailor-made pH gradient was developed. The latter approach was used in Paper IV for preconcentration and purification of Aβ peptides after immunoprecipitation from cerebrospinal fluid and blood plasma, followed by MALDI-MS from a micropillar chip. Paper V includes simulations of an isotachophoretic strategy for selective enrichment of Aβ peptides. GENTRANS simulations were used to select the electrolyte composition, and 2D simulations in a geometry suitable for on-chip implementation were performed using COMSOL Multiphysics.

QC 20160930

Zhang, Qishan, and 张绮珊. "Investigating biological mechanisms for the induction of autophagy in neurons stressed by beta-amyloid peptides." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2012. http://hdl.handle.net/10722/193067.

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Alzheimer’s disease (AD) is an age-related neurodegenerative disorder, characterized by global cognitive decline and progressive memory loss. As many other neurological disorders characterized by “proteinopathy”, pathology of AD includes beta-amyloid plaques and tau neurofibrillary tangles, which imply a crucial role of the cellular degradation systems in maintaining homeostasis of protein turnover. This is especially important for post-mitotic neuronal cells since aggravating protein crisis cannot be alleviated by cell division. Autophagy is a cellular degradation process that removes or recycles long-lived proteins and damaged organelles, with its enhancement being remarkably implicated during the progression of Alzheimer’s disease (AD). The majority of studies have hitherto focused on the mechanism of how oligomeric Ah, as one of the potent toxic species in AD, activates autophagy. However, how autophagy is activated remains to be elucidated. The goal of this study is to reveal the underlying mechanisms of autophagy and the subsequent events. Using imaging and biochemical analysis in primary cultures of rat hippocampal neurons, I found that oligomeric An-induced autophagy was initiated by aggregation of the endoplasmic reticulum (ER), in an mTOR-independent pathway. Ao-triggered autophagosomes were derived from omegasomes, starting from the ER aggregation sites. Aggregation of the ER facilitated the clustering of Atg14L to propel the recruitment of Beclin1 and Vps34, which contributes to generation of omegasomes. I further found that p62 targeted to ER aggregates possibly through the enhanced ubiquitinated ER chaperones trapped at ER aggregation sites, implicating the underlying mechanism for how p62 are recruited to autophagosome formation sites (omegasomes). Herein, I report key steps for activation of AH-triggered autophagy, whereby a mechanistic link between ER aggregation, autophagic activation and recruitment of p62 to autophagosome formation sites is revealed. First, Ao-induced ER aggregation triggers autophagy, via the recruitment of Beclin 1 and Vps34 to Atg14L clusters, which is a promoting factor for omegasome formation at the ER aggregation site. Second, the recruitment of p62 to omegasomes is likely mediated by the attraction of the underlying accumulation of ubiquitinated ER chaperones at the ER aggregation site. Up-regulation of autophagy is an early sign of AD. The activation of autophagy without tightly manipulation may contribute to neuronal damage in AD. In addition, how the autophagic substrates can be efficiently incorporated into the autophagic pathway is important for understanding the sustainability of autophagy. Therefore, my study on elucidating how ER aggregation initiates autophagy and the autophagic substrate/cargo receptor p62 are loaded onto autophagosome formation sites may help us to identify a potential therapeutic strategy or target for AD patients.
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Anatomy
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Doctor of Philosophy

Bautista, Mahealani Roberts. "Identification and design of small molecules that associate with aggregated Alzheimer's-related beta-amyloid peptides." Diss., [La Jolla, Calif.] : University of California, San Diego, 2009. http://wwwlib.umi.com/cr/ucsd/fullcit?p3344755.

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Thesis (Ph. D.)--University of California, San Diego, 2009.
Title from first page of PDF file (viewed Apr. 3, 2009). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (p. 178-202).

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Книги з теми "Beta-Amyloid peptides":

Indu, Kheterpal, and Wetzel Ronald, eds. Amyloid, prions, and other protein aggregates Part C. Amsterdam: Elsevier/Academic, 2006.

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Indu, Kheterpal, and Wetzel Ronald, eds. Amyloid, prions, and other protein aggregates Part B. Amsterdam: Elsevier/Academic, 2006.

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C, Dowler Brynn, ed. Endocytosis: Structural components, functions, and pathways. Hauppauge, N.Y: Nova Science Publishers, 2010.

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Tanzi, Rudolph E. Decoding darkness: The search for the genetic causes of Alzheimer's disease. Cambridge, Mass: Perseus Pub., 2000.

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A, Nixon Ralph, Banner Carl D. B, and New York Academy of Sciences., eds. Proteases and protease inhibitors in Alzheimer's disease pathogenesis. New York: NewYork Academy of Sciences, 1992.

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B, Banner Carl D., and Nixon Ralph A, eds. Proteases and protease inhibitors in Alzheimer's disease pathogenesis. New York, N.Y: New York Academy of Sciences, 1992.

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Wetzel, Ronald, and Indu Kheterpal. Amyloid, Prions, and Other Protein Aggregates, Part C. Elsevier Science & Technology Books, 2006.

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(Editor), Ronald Wetzel, and Indu Kheterpal (Editor), eds. Amyloid, Prions, and Other Protein Aggregates, Part C, Volume 413 (Methods in Enzymology). Academic Press, 2006.

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Abelson, John N., Ronald Wetzel, and Melvin I. Simon. Amyloid, Prions, and Other Protein Aggregates. Elsevier Science & Technology Books, 1999.

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(Editor), Ronald Wetzel, and Indu Kheterpal (Editor), eds. Amyloid, Prions, and Other Protein Aggregates, Part B, Volume 412 (Methods in Enzymology). Academic Press, 2006.

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Частини книг з теми "Beta-Amyloid peptides":

Durieux, J. P., F. Dick, M. Schwaller, G. Haas, U. Wixmerten, S. Mundwiler, and R. Nyfeler. "Synthesis of beta amyloid protein [1-40] scope and limitations of convergent solid phase synthesis." In Peptides, 34–36. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0683-2_4.

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Benseny-Cases, Núria, Oksana Klementieva, and Josep Cladera. "In vitroOligomerization and Fibrillogenesis of Amyloid-beta Peptides." In Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease, 53–74. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-5416-4_3.

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Takahashi, Eddie, Anita Howe, Ole Vesterqvist, and Zhaosheng Lin. "Quantitation of Amyloid Beta Peptides in CSF by Surface Enhanced MALDI-TOF." In Methods in Molecular Biology, 227–36. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-61779-418-6_16.

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Lahiri, Debomoy K., and Martin R. Farlow. "Tacrine Reduces the Secretion of Soluble Amyloid Beta-Peptides in a Neuroblastoma Cell Line." In Advances in Behavioral Biology, 563–69. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5337-3_80.

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Kondela, Tomáš, Pavol Hrubovčák, Dmitry Soloviov, Dina Badreeva, Tatiana Murugova, Vadim Skoi, Alexander Kuklin, Oleksandr Ivankov, and Norbert Kučerka. "Approaches for a Closer Look at Problems of Liquid Membranes with Amyloid-Beta Peptides." In Springer Proceedings in Physics, 265–94. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-80924-9_10.

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Beffert, Uwe, Nicole Aumont, Doris Dea, Jean Davignon, and Judes Poirier. "Apolipoprotein E Uptake is Increased by Beta-Amyloid Peptides and Reduced by Blockade of the LDL Receptor." In Neurodegenerative Diseases, 103–8. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4899-0209-2_15.

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Okochi, M., A. Fukumori, Y. Satoh, N. Aidaralieva, H. Tanii, K. Kamino, T. Tanaka, T. Kudo, and M. Takeda. "Alzheimer�s γ-Secretase Mechanism Produces Amyloid-β-Protein Like Peptides Simultaneously with Release of Intracellular Signaling Fragments." In Molecular Neurobiology of Alzheimer Disease and Related Disorders, 31–41. Basel: KARGER, 2004. http://dx.doi.org/10.1159/000078524.

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Kumar, Suresh, Edward J. Okello, and J. Robin Harris. "Experimental Inhibition of Fibrillogenesis and Neurotoxicity by amyloid-beta (Aβ) and Other Disease-Related Peptides/Proteins by Plant Extracts and Herbal Compounds." In Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease, 295–326. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-5416-4_13.

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Abraham, Carmela R. "Amyloid Beta Peptide and the Amyloid Cascade Hypothesis." In The Handbook of Alzheimer's Disease and Other Dementias, 262–76. Oxford, UK: Wiley-Blackwell, 2011. http://dx.doi.org/10.1002/9781444344110.ch8.

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Kagan, Bruce L., and Jyothi Thundimadathil. "Amyloid Peptide Pores and the Beta Sheet Conformation." In Advances in Experimental Medicine and Biology, 150–67. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6327-7_13.

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Тези доповідей конференцій з теми "Beta-Amyloid peptides":

Drochioiu, Gabi, Manuela Murariu, Laura Ion, and Laura Habasescu. "Iron and aluminum interaction with amyloid-beta peptides associated with Alzheimer’s disease." In INTERNATIONAL CONFERENCE OF COMPUTATIONAL METHODS IN SCIENCES AND ENGINEERING 2014 (ICCMSE 2014). AIP Publishing LLC, 2014. http://dx.doi.org/10.1063/1.4897686.

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Ion, Laura, Monica Jureschi, Ancuta Lupaescu, Brindusa-Alina Petre, and Gabi Drochioiu. "METAL IONS BINDING TO AMYLOID-BETA AND NEUROPROTECTIVE NAP-LIKE PEPTIDES: MS, FT-IR AND AFM INVESTIGATIONS." In 20th International Multidisciplinary Scientific GeoConference Proceedings SGEM 2020. STEF92 Technology, 2020. http://dx.doi.org/10.5593/sgem2020/6.1/s25.034.

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Ki-Bong Song, Chang-Bum Kim, and Yo-Han Choi. "Sensing and quantification of salivary beta-amyloid peptides and protein sequencing for the saliva of normal and AD patients." In 2015 IEEE Sensors. IEEE, 2015. http://dx.doi.org/10.1109/icsens.2015.7370592.

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Mendonça, Pedro Henrique Carvalho Furtado de, Fernanda Rabello Detoni, Letícia Silva Brandão dos Santos, Talita Cardoso Gomes, and Ivan Magalhães Viana. "Monoclonal antibodies in the treatment of Alzheimer’s disease: a literature review." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.597.

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Background: Alzheimer’s disease (AD) is a neurodegenerative disorder, whose treatment is limited to drugs that offer comfort to the patient. Immunotherapy with monoclonal antibodies (mAbs) has been the subject of a study with the promise of reversing cognitive deficits. In this scenario, we conducted a systematic review to elucidate aspects about the effectiveness of such treatment. Objectives: Analyze the prognostic of patients with AD through immunotherapy using anti-amilody mAbs. Methods: It was used the PubMed database using the descriptors: “Amyloid beta-Peptides AND Alzheimer disease AND Immunotherapy”. Filters: clinical trial, randomized controlled trial. 6 articles from 2015 to 2021 were selected. Inclusion criteria: (1) mAbs as treatment for AD; (2) Analyze the prognostic. Results: The immunotherapy with bapineuzumab and solanezumab didn’t showed no statistically significant difference between the groups of bapineuzumab 0,5 mg / kg (p = 0,979) and placebo (p = 0,973) and a change of 6.65 in the solanezumab group and 7.44 in the placebo group (difference, −0.80; P = 0 , 10). However, subcutaneous treatment of bapineuzumab exhibited fewer abnormalities of images related to amyloid with edema or effusion (AIRA), so, better tolerated compared to intravenous treatment. In the study with the ABvac40 vaccine, about 92% of the individuals in the test group developed specific anti-Aβ 40 antibodies. Conclusion: Bapineuzumab and solanezumab didn’t achieve significant results in the reduction of cognitive decline, however bapineuzumab enabled the prevention of Aβ aggregation. However, the use of mAbs can trigger collateral effects, requiring an individual analysis.

Volkova, Tatiana Danilovna, Armine Vrezovna Avetisyan, Dmitry Otarovich Koroev, and Olga Volpina. "PROTECTIVE RAGE FRAGMENT INHIBITS AMYLOID BETA OLIGOMERIZATION." In NEW TECHNOLOGIES IN MEDICINE, BIOLOGY, PHARMACOLOGY AND ECOLOGY. Institute of information technology, 2021. http://dx.doi.org/10.47501/978-5-6044060-1-4.19.

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The article discusses the involvement of beta-amyloid in the mechanism of the protective action of the synthetic RAGE fragment. It was shown that the peptide is able to suppress the formation of oligomers and fibrils of beta-amyloid in solution. This confirms the hypothesis that the protective activity of the peptide is associated with its ability to inhibit the process of oligomerization of beta-amyloid.

Kissoon, Nicola N., Andre´s D. Gutierrez, Anant K. Paravastu, and Ongi Englander. "Preparation and Integration of Beta Amyloid Protein Nanofibers With Microfabricated Electrodes." In ASME 2010 International Mechanical Engineering Congress and Exposition. ASMEDC, 2010. http://dx.doi.org/10.1115/imece2010-38360.

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Micro and nano fabricated bio-systems and bio-devices can be produced once compatible processes for the integration of biomaterials and micro and nano systems are developed. Here, we demonstrate the integration of Alzheimer’s β-amyloid peptide nanofibers with metalized electrodes. The metalized electrodes and Alzheimer’s β-amyloid peptide nanofiber solutions are prepared separately. Metalized electrodes, composed of either chrome/gold or aluminum, with multiple electrodes are prepared using standard photolithography processes. Meanwhile, the Alzheimer’s β-amyloid peptide nanofiber solutions are prepared via the hydration of β-amyloid powder at various concentrations. The self-assembly of the β-amyloid nanofibers, to achieve well-dispersed networks, is optimized through periodic sonication and readdition of aliquots over timed intervals. The β-amyloid peptide solution can be successfully deposited onto the metalized electrodes to yield dense yet well-dispersed nanofiber arrays.

Carneiro, P., C. Delerue-Matos, S. Morais, and Maria do Carmo Pereira. "Electrochemical immunosensor for amyloid beta-peptide detection: Preliminary study." In 2013 IEEE 3rd Portuguese Meeting in Bioengineering (ENBENG). IEEE, 2013. http://dx.doi.org/10.1109/enbeng.2013.6518403.

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Andrade, Stephanie, Joana A. Loureiro, Manuel A. N. Coelho, and Maria do Carmo Pereira. "Interaction studies of amyloid beta-peptide with the natural compound resveratrol." In 2015 IEEE 4th Portuguese Meeting on Bioengineering (ENBENG). IEEE, 2015. http://dx.doi.org/10.1109/enbeng.2015.7088833.

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"The study of localization of beta-amyloid peptide monomers in cells by fluorescence microscopy." In Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-188.

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Gonçalves, Brenda, Isadora Ribeiro, Thamires Magalhães, Christian Gerbelli, Luciana Pimentel Silva, Helena Joaquim, Leda Talib, Orestes Forlenza, and Marcio Balthazar. "NEUROPSYCHOLOGICAL TESTS AS PREDICTORS OF CONVERSION TO ALZHEIMER’S DISEASE IN BETA-AMYLOID POSITIVE INDIVIDUALS." In XIII Meeting of Researchers on Alzheimer's Disease and Related Disorders. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1980-5764.rpda007.

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Background: amnestic Mild Cognitive Impairment (aMCI) refers to a possibletransitional stage between healthy aging and dementia and has an increased chance of converting to Alzheimer’s disease (AD). Objectives: to assess whether neuropsychological tests can predict the conversion to AD in patients with aMCI and altered CSF amyloid peptide (βA+). Methods: 48 individuals underwent neuropsychological assessment (time 0 and time 1), being 18 healthy controls and 30 aMCI βA+, who performed a single CSF collection (time 0). All subjects with aMCI scored 0.5 in the Memory category of the Clinical Dementia Rating (CDR) test, and we considered the conversion to AD if the overall score changed from 0.5 to 1. We performed different additional univariate analyses with MANOVAs to differentiate between groups. Results : 8 subjects converted to AD (converters), and 22 remained stable (non-converters). The converters performed worse in the sub-item test Recognition of Rey Auditory Verbal Learning Test (RAVLT) compared to controls and non-converters (F = 14,58, p <0,001). Conclusions: the Recognition task of the RAVLT was able to differentiate aMCI βA+ individuals who converted to AD in our sample, which was not observed in the other investigated tests. We suggest additional studies with larger sample sizes and validation cohorts to contribute to our findings.