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Relevant bibliographies by topics / Β-amyloid structures

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Academic literature on the topic 'Β-amyloid structures'

Author: Grafiati

Published: 23 November 2024

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Journal articles on the topic "Β-amyloid structures"

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Taguchi, Yuzuru, Hiroki Otaki, and Noriyuki Nishida. "Mechanisms of Strain Diversity of Disease-Associated in-Register Parallel β-Sheet Amyloids and Implications About Prion Strains." Viruses 11, no. 2 (January 28, 2019): 110. http://dx.doi.org/10.3390/v11020110.

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The mechanism of prion strain diversity remains unsolved. Investigation of inheritance and diversification of protein-based pathogenic information demands the identification of the detailed structures of abnormal isoforms of the prion protein (PrPSc); however, achieving purification is difficult without affecting infectivity. Similar prion-like properties are recognized also in other disease-associated in-register parallel β-sheet amyloids including Tau and α-synuclein (αSyn) amyloids. Investigations into structures of those amyloids via solid-state nuclear magnetic resonance spectroscopy and cryo-electron microscopy recently made remarkable advances due to their relatively small sizes and lack of post-translational modifications. Herein, we review advances regarding pathogenic amyloids, particularly Tau and αSyn, and discuss implications about strain diversity mechanisms of prion/PrPSc from the perspective that PrPSc is an in-register parallel β-sheet amyloid. Additionally, we present our recent data of molecular dynamics simulations of αSyn amyloid, which suggest significance of compatibility between β-sheet propensities of the substrate and local structures of the template for stability of amyloid structures. Detailed structures of αSyn and Tau amyloids are excellent models of pathogenic amyloids, including PrPSc, to elucidate strain diversity and pathogenic mechanisms.

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Chatani, Eri, Keisuke Yuzu, Yumiko Ohhashi, and Yuji Goto. "Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils." International Journal of Molecular Sciences 22, no. 9 (April 21, 2021): 4349. http://dx.doi.org/10.3390/ijms22094349.

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Amyloid fibrils are supramolecular protein assemblies represented by a cross-β structure and fibrous morphology, whose structural architecture has been previously investigated. While amyloid fibrils are basically a main-chain-dominated structure consisting of a backbone of hydrogen bonds, side-chain interactions also play an important role in determining their detailed structures and physicochemical properties. In amyloid fibrils comprising short peptide segments, a steric zipper where a pair of β-sheets with side chains interdigitate tightly is found as a fundamental motif. In amyloid fibrils comprising longer polypeptides, each polypeptide chain folds into a planar structure composed of several β-strands linked by turns or loops, and the steric zippers are formed locally to stabilize the structure. Multiple segments capable of forming steric zippers are contained within a single protein molecule in many cases, and polymorphism appears as a result of the diverse regions and counterparts of the steric zippers. Furthermore, the β-solenoid structure, where the polypeptide chain folds in a solenoid shape with side chains packed inside, is recognized as another important amyloid motif. While side-chain interactions are primarily achieved by non-polar residues in disease-related amyloid fibrils, the participation of hydrophilic and charged residues is prominent in functional amyloids, which often leads to spatiotemporally controlled fibrillation, high reversibility, and the formation of labile amyloids with kinked backbone topology. Achieving precise control of the side-chain interactions within amyloid structures will open up a new horizon for designing useful amyloid-based nanomaterials.

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Paulus, Agnes, Anders Engdahl, Yiyi Yang, Antonio Boza-Serrano, Sara Bachiller, Laura Torres-Garcia, Alexander Svanbergsson, et al. "Amyloid Structural Changes Studied by Infrared Microspectroscopy in Bigenic Cellular Models of Alzheimer’s Disease." International Journal of Molecular Sciences 22, no. 7 (March 26, 2021): 3430. http://dx.doi.org/10.3390/ijms22073430.

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Alzheimer’s disease affects millions of lives worldwide. This terminal disease is characterized by the formation of amyloid aggregates, so-called amyloid oligomers. These oligomers are composed of β-sheet structures, which are believed to be neurotoxic. However, the actual secondary structure that contributes most to neurotoxicity remains unknown. This lack of knowledge is due to the challenging nature of characterizing the secondary structure of amyloids in cells. To overcome this and investigate the molecular changes in proteins directly in cells, we used synchrotron-based infrared microspectroscopy, a label-free and non-destructive technique available for in situ molecular imaging, to detect structural changes in proteins and lipids. Specifically, we evaluated the formation of β-sheet structures in different monogenic and bigenic cellular models of Alzheimer’s disease that we generated for this study. We report on the possibility to discern different amyloid signatures directly in cells using infrared microspectroscopy and demonstrate that bigenic (amyloid-β, α-synuclein) and (amyloid-β, Tau) neuron-like cells display changes in β-sheet load. Altogether, our findings support the notion that different molecular mechanisms of amyloid aggregation, as opposed to a common mechanism, are triggered by the specific cellular environment and, therefore, that various mechanisms lead to the development of Alzheimer’s disease.

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Sulatskaya, Anna I., Anastasiia O. Kosolapova, Alexander G. Bobylev, Mikhail V. Belousov, Kirill S. Antonets, Maksim I. Sulatsky, Irina M. Kuznetsova, Konstantin K. Turoverov, Olesya V. Stepanenko, and Anton A. Nizhnikov. "β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis." International Journal of Molecular Sciences 22, no. 21 (October 20, 2021): 11316. http://dx.doi.org/10.3390/ijms222111316.

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Insoluble protein aggregates with fibrillar morphology called amyloids and β-barrel proteins both share a β-sheet-rich structure. Correctly folded β-barrel proteins can not only function in monomeric (dimeric) form, but also tend to interact with one another—followed, in several cases, by formation of higher order oligomers or even aggregates. In recent years, findings proving that β-barrel proteins can adopt cross-β amyloid folds have emerged. Different β-barrel proteins were shown to form amyloid fibrils in vitro. The formation of functional amyloids in vivo by β-barrel proteins for which the amyloid state is native was also discovered. In particular, several prokaryotic and eukaryotic proteins with β-barrel domains were demonstrated to form amyloids in vivo, where they participate in interspecies interactions and nutrient storage, respectively. According to recent observations, despite the variety of primary structures of amyloid-forming proteins, most of them can adopt a conformational state with the β-barrel topology. This state can be intermediate on the pathway of fibrillogenesis (“on-pathway state”), or can be formed as a result of an alternative assembly of partially unfolded monomers (“off-pathway state”). The β-barrel oligomers formed by amyloid proteins possess toxicity, and are likely to be involved in the development of amyloidoses, thus representing promising targets for potential therapy of these incurable diseases. Considering rapidly growing discoveries of the amyloid-forming β-barrels, we may suggest that their real number and diversity of functions are significantly higher than identified to date, and represent only “the tip of the iceberg”. Here, we summarize the data on the amyloid-forming β-barrel proteins, their physicochemical properties, and their biological functions, and discuss probable means and consequences of the amyloidogenesis of these proteins, along with structural relationships between these two widespread types of β-folds.

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Alperstein, Ariel M., Joshua S. Ostrander, Tianqi O. Zhang, and Martin T. Zanni. "Amyloid found in human cataracts with two-dimensional infrared spectroscopy." Proceedings of the National Academy of Sciences 116, no. 14 (March 20, 2019): 6602–7. http://dx.doi.org/10.1073/pnas.1821534116.

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UV light and other factors damage crystallin proteins in the eye lens, resulting in cataracts that scatter light and affect vision. Little information exists about protein structures within these disease-causing aggregates. We examined postmortem lens tissue from individuals with and without cataracts using 2D infrared (2DIR) spectroscopy. Amyloid β-sheet secondary structure was detected in cataract lenses along with denatured structures. No amyloid structures were found in lenses from juveniles, but mature lenses with no cataract diagnosis also contained amyloid, indicating that amyloid structures begin forming before diagnosis. Light scatters more strongly in regions with amyloid structure, and UV light induces amyloid β-sheet structures, linking the presence of amyloid structures to disease pathology. Establishing that age-related cataracts involve amyloid structures gives molecular insight into a common human affliction and provides a possible structural target for pharmaceuticals as an alternative to surgery.

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Freitas, Raul O., Adrian Cernescu, Anders Engdahl, Agnes Paulus, João E. Levandoski, Isak Martinsson, Elke Hebisch, et al. "Nano-Infrared Imaging of Primary Neurons." Cells 10, no. 10 (September 27, 2021): 2559. http://dx.doi.org/10.3390/cells10102559.

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Alzheimer’s disease (AD) accounts for about 70% of neurodegenerative diseases and is a cause of cognitive decline and death for one-third of seniors. AD is currently underdiagnosed, and it cannot be effectively prevented. Aggregation of amyloid-β (Aβ) proteins has been linked to the development of AD, and it has been established that, under pathological conditions, Aβ proteins undergo structural changes to form β-sheet structures that are considered neurotoxic. Numerous intensive in vitro studies have provided detailed information about amyloid polymorphs; however, little is known on how amyloid β-sheet-enriched aggregates can cause neurotoxicity in relevant settings. We used scattering-type scanning near-field optical microscopy (s-SNOM) to study amyloid structures at the nanoscale, in individual neurons. Specifically, we show that in well-validated systems, s-SNOM can detect amyloid β-sheet structures with nanometer spatial resolution in individual neurons. This is a proof-of-concept study to demonstrate that s-SNOM can be used to detect Aβ-sheet structures on cell surfaces at the nanoscale. Furthermore, this study is intended to raise neurobiologists’ awareness of the potential of s-SNOM as a tool for analyzing amyloid β-sheet structures at the nanoscale in neurons without the need for immunolabeling.

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Yu, Xiang, and Jie Zheng. "Polymorphic Structures of Alzheimer's β-Amyloid Globulomers." PLoS ONE 6, no. 6 (June 7, 2011): e20575. http://dx.doi.org/10.1371/journal.pone.0020575.

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Yakupova, Elmira I., Liya G. Bobyleva, Sergey A. Shumeyko, Ivan M. Vikhlyantsev, and Alexander G. Bobylev. "Amyloids: The History of Toxicity and Functionality." Biology 10, no. 5 (May 1, 2021): 394. http://dx.doi.org/10.3390/biology10050394.

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Proteins can perform their specific function due to their molecular structure. Partial or complete unfolding of the polypeptide chain may lead to the misfolding and aggregation of proteins in turn, resulting in the formation of different structures such as amyloid aggregates. Amyloids are rigid protein aggregates with the cross-β structure, resistant to most solvents and proteases. Because of their resistance to proteolysis, amyloid aggregates formed in the organism accumulate in tissues, promoting the development of various diseases called amyloidosis, for instance Alzheimer’s diseases (AD). According to the main hypothesis, it is considered that the cause of AD is the formation and accumulation of amyloid plaques of Aβ. That is why Aβ-amyloid is the most studied representative of amyloids. Therefore, in this review, special attention is paid to the history of Aβ-amyloid toxicity. We note the main problems with anti-amyloid therapy and write about new views on amyloids that can play positive roles in the different organisms including humans.

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Tycko, Robert. "Molecular structure of amyloid fibrils: insights from solid-state NMR." Quarterly Reviews of Biophysics 39, no. 1 (February 2006): 1–55. http://dx.doi.org/10.1017/s0033583506004173.

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1. Introduction 22. Sources of structural information in solid-state NMR data 52.1 General remarks 52.2 Chemical shifts, linewidths, and magic-angle spinning 62.3 Dipole–dipole couplings and dipolar recoupling 82.4 Tensor correlation techniques 122.5 Solid-state NMR of aligned samples 142.6 Indirect sources of structural information 152.7 Sample preparation for solid-state NMR 153. Levels of structure in amyloid fibrils 184. Molecular structure of β-amyloid fibrils 254.1 Self-propagating, molecular-level polymorphism in Aβ1–40 fibrils 254.2 Structural model for Aβ1-40 fibrils 284.3 Staggering of β-strands in Aβ1-40 fibrils 324.4 Structure of Aβ1-42 fibrils 344.5 Structure of fibrils formed by short β-amyloid fragments 344.6 Structures of non-fibrillar aggregates 355. Molecular structure of other amyloid fibrils 365.1 Ure2p10–39 and full-length Ure2p fibrils 365.2 TTR105–115 fibrils 385.3 HET-s fibrils 385.4 Amylin fibrils 395.5 PrP fibrils 395.6 ccβ fibrils 405.7 α-synuclein fibrils 405.8 Calcitonin fibrils 416. Data relevant to various proposals regarding amyloid structure 416.1 β-helical models for amyloid fibrils 416.2 Amyloid fibrils as water-filled nanotubes 426.3 Domain swapping in amyloid fibrils 426.4 The parallel superpleated β-structure model 436.5 α-sheet structures in amyloid fibrils 437. Conclusions 448. Acknowledgments 469. References 46Solid-state nuclear magnetic resonance (NMR) measurements have made major contributions to our understanding of the molecular structures of amyloid fibrils, including fibrils formed by the β-amyloid peptide associated with Alzheimer's disease, by proteins associated with fungal prions, and by a variety of other polypeptides. Because solid-state NMR techniques can be used to determine interatomic distances (both intramolecular and intermolecular), place constraints on backbone and side-chain torsion angles, and identify tertiary and quaternary contacts, full molecular models for amyloid fibrils can be developed from solid-state NMR data, especially when supplemented by lower-resolution structural constraints from electron microscopy and other sources. In addition, solid-state NMR data can be used as experimental tests of various proposals and hypotheses regarding the mechanisms of amyloid formation, the nature of intermediate structures, and the common structural features within amyloid fibrils. This review introduces the basic experimental and conceptual principles behind solid-state NMR methods that are applicable to amyloid fibrils, reviews the information about amyloid structures that has been obtained to date with these methods, and discusses how solid-state NMR data provide insights into the molecular interactions that stabilize amyloid structures, the generic propensity of polypeptide chains to form amyloid fibrils, and a number of related issues that are of current interest in the amyloid field.

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Flynn, Jessica D., and Jennifer C. Lee. "Raman fingerprints of amyloid structures." Chemical Communications 54, no. 51 (2018): 6983–86. http://dx.doi.org/10.1039/c8cc03217c.

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Dissertations / Theses on the topic "Β-amyloid structures"

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Newby, Francisco Nicolas. "Structural studies of the Alzheimer's amyloid β peptide." Thesis, University of Cambridge, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.607712.

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Siegemund, Thomas. "Structure and properties of drug-loaded polymeric nanoparticles targeting β-amyloid." Doctoral thesis, Universitätsbibliothek Leipzig, 2011. http://nbn-resolving.de/urn:nbn:de:bsz:15-qucosa-70212.

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Polymere Nanopartikel sind ein vielversprechender Ansatz für die Diagnose und Therapie von Krankheiten. Sie ermöglichen den Einsatz von schwerlöslichen oder instabilen Wirkstoffen. Ein weiterer Vorteil ist die Möglichkeit das Targetings, durch gezielte Modifikationen des Nanopartikels wird der Wirkstoff zum Zielort transportiert und kann dort in der gewünschten Form freigesetzt werden; dadurch könnten bei erhöhter Wirksamkeit die Nebenwirkungen von Medikamenten reduziert werden. Ziel dieser Arbeit war die Untersuchung von physikalischen und biochemischen Eigenschaften von Nanopartikeln bestehend aus einem abbaustabilen Polystyren- Kern und einer biologisch abbaubaren Schale aus Polybutylcyanoacrylat. Es werden Methoden beschrieben, um die Größe, Struktur und den Abbau dieser Wirkstoffträger zu untersuchen. Die untersuchten Nanopartikel zeigen RAYLEIGH-Streuung, sowohl Größe als auch Abbau können durch Messung des Absorptionsspektrums bestimmt werden. Weiterhin konnten diese Eigenschaften mit Hilfe von dynamischer und statischer Lichtstreuung sowie Neutronenkleinwinkelstreuung untersucht werden. Bei letzterer Methode konnte gezeigt werden, dass die Schale größtenteils abgebaut werden kann, während der Kern intakt bleibt. In einem weiteren Teil der Arbeit wurde die Überwindung der Blut-Hirn-Schranke durch polymere Nanopartikel untersucht. Dabei wurde der fluoreszierende Thioflavine als Modellwirkstoffe eingesetzt. Das Durchdringen der Blut-Hirn-Schranke konnte nur mit Nanopartikeln erreicht werden, an deren Oberfläche ein Apolipoprotein E-Peptid gekoppelt war. Es konnte gezeigt werden, das die Nanopartikelschale im Gehirn abgebaut wird, der Wirkstoff freigesetzt wird und an Amyloid β, einem Marker der Alzheimer-Krankheit, bindet.

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Daou, Dania. "Intégration de moteurs moléculaires photoactivables dans des gels supramoléculaires." Electronic Thesis or Diss., Strasbourg, 2024. http://www.theses.fr/2024STRAF021.

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Cette thèse a exploré l'intégration de moteurs moléculaires synthétiques photoactivables dans des réseaux de gels supramoléculaires. L'objectif principal était d'obtenir un mouvement macroscopique réversible en exploitant à la fois la rotation unidirectionnelle des moteurs moléculaires et la nature réversible des interactions supramoléculaires. Des moteurs moléculaires hautement fonctionnalisés ont été synthétisés et intégrés comme unités de réticulation dans des réseaux de gel supramoléculaire de peptides de diphénylalanine et de poly(γ-benzyl-L-glutamate) et d'oligonucléotides d'ADN. L'activation de la rotation unidirectionnelle des moteurs moléculaires par la lumière a permis de produire un travail nanomécanique suffisant pour perturber les interactions supramoléculaires dans les réseaux de gel à base de peptides, ce qui entraîne la contraction ou la fonte du gel à l'échelle macroscopique. Grâce aux interactions supramoléculaires réversibles, le matériau gélifié initial a pu être récupéré dans l'obscurité, soit spontanément, soit par l'application d'un stimulus thermique. Les systèmes étudiés dans cette thèse représentent une nouvelle classe de matériaux fonctionnant dans des conditions dissipatives hors équilibre, promettant des applications dans divers domaines tels que la biologie, la médecine et la science des matériaux
This thesis explored the integration of light-driven synthetic molecular motors in supramolecular gel networks. The main goal was to achieve reversible macroscopic motion by exploiting both the unidirectional rotation of molecular motors and the reversible nature of supramolecular interactions. Highly functionalized molecular motors have been synthesized and integrated as crosslinking units in supramolecular gel networks of diphenylalanine and poly(γ- benzyl-L-glutamate) peptides, as well as DNA oligonucleotides. Activation of the unidirectional rotation of molecular motors by light, allowed the production of nanomechanical work which is sufficient to disrupt supramolecular interactions in peptide-based gel networks leading to contraction or melting of the gel material at the macroscopic scale. Thanks to the reversible supramolecular interactions, the initial gel material was recovered in the dark, either spontaneously or by applying a thermal stimulus. The systems studied in this thesis represent a novel class of materials operating in dissipative out-of-equilibrium conditions, holding promise of applications in various fields such as biology, medicine and material science

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Zhu, Maximillian. "Computational studies of the Alzheimer's amyloid-β peptide : from structural ensembles to therapeutic leads." Thesis, University of Cambridge, 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.608056.

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Cozma, Claudia [Verfasser]. "Determination of Primary Structure and Affinity Characterization of Naturally Occurring β-Amyloid Autoantibodies / Claudia Cozma." Konstanz : Bibliothek der Universität Konstanz, 2014. http://d-nb.info/1079910271/34.

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Wißbrock, Amelie [Verfasser]. "Transient Heme-Protein Interactions: Structural and Functional Studies on Interleukin-36α and Amyloid-β / Amelie Wißbrock." Bonn : Universitäts- und Landesbibliothek Bonn, 2020. http://d-nb.info/1224270444/34.

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Paraschiv, Gabriela Ioana [Verfasser]. "Structural identification and quantification of β-amyloid polypeptide-ligand interactions using affinity-mass spectrometric methods / Gabriela Ioana Paraschiv." Konstanz : Bibliothek der Universität Konstanz, 2012. http://d-nb.info/1025637240/34.

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Cerda, Muñoz Fabian Esteban [Verfasser], Wolfgang [Akademischer Betreuer] Baumeister, Bernd [Gutachter] Reif, and Wolfgang [Gutachter] Baumeister. "Structural study of the Amyloid β cytotoxicity / Fabian Esteban Cerda Muñoz ; Gutachter: Bernd Reif, Wolfgang Baumeister ; Betreuer: Wolfgang Baumeister." München : Universitätsbibliothek der TU München, 2021. http://d-nb.info/1230552790/34.

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Dammers, Christina [Verfasser], Dieter [Gutachter] Willbold, and Henrike [Gutachter] Heise. "Structural analysis and aggregation of Alzheimer’s disease related pyroglutamate-modified amyloid-β / Christina Dammers ; Gutachter: Dieter Willbold, Henrike Heise." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2017. http://d-nb.info/1132771757/34.

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Dammers, Christina Verfasser], Dieter [Gutachter] [Willbold, and Henrike [Gutachter] Heise. "Structural analysis and aggregation of Alzheimer’s disease related pyroglutamate-modified amyloid-β / Christina Dammers ; Gutachter: Dieter Willbold, Henrike Heise." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2017. http://d-nb.info/1132771757/34.

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Book chapters on the topic "Β-amyloid structures"

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Tycko, Robert. "β-Amyloid Fibril Structures, In Vitro and In Vivo." In Proteopathic Seeds and Neurodegenerative Diseases, 19–31. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-35491-5_2.

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Bukauskas, V., V. Strazdienė, A. Šetkus, S. Bružytė, V. Časaitė, and R. Meškys. "β-Sheeted Amyloid Fibril Based Structures For Hybrid Nanoobjects On Solid Surfaces." In Springer Proceedings in Physics, 61–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-95930-4_10.

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van Andel, A. C. J., P. R. Hol, J. H. van der Maas, E. T. G. Lutz, H. Krabbendam, and E. Gruys. "Reaggregation of Bovine Amyloid a Fibril Components to β-Pleated Sheet Fibrillar Structures." In Amyloidosis, 39–48. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2199-6_5.

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Inouye, Hideyo, and Daniel A. Kirschner. "Refined Fibril Structures: The Hydrophobic Core in Alzheimer's Amyloid β-Protein and Prion as Revealed by X-ray Diffraction." In Novartis Foundation Symposia, 22–46. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514924.ch3.

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Muñoz, Francisco J., and Nibaldo C. Inestrosa. "Acetylcholinesterase Enhances the Neurotoxicity of β-Amyloid Fibrils." In Structure and Function of Cholinesterases and Related Proteins, 182. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1540-5_48.

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Meier, Beat H., and Anja Böckmann. "Solid-State NMR Structure of Amyloid-β Fibrils." In Methods in Molecular Biology, 53–62. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2597-2_5.

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De Ferrari, Giancarlo V., and Nibaldo C. Inestrosa. "Identification of an Acetylcholinesterase Fragment that Promotes Alzheimer β-Amyloid Fibril Formation." In Structure and Function of Cholinesterases and Related Proteins, 185–86. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1540-5_50.

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Gröbner, Gerhard, Clemens Glaubitz, Philip T. F. Williamson, Timothy Hadingham, and Anthony Watts. "Structural insight into the interaction of amyloid-β peptide with biological membranes by solid state NMR." In Focus on Structural Biology, 203–14. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-017-2579-8_18.

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Pateras, Joseph, Ashwin Vaidya, and Preetam Ghosh. "Physics-Informed Bias Method for Multiphysics Machine Learning: Reduced Order Amyloid-β Fibril Aggregation." In Recent Advances in Mechanics and Fluid-Structure Interaction with Applications, 157–65. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-14324-3_7.

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Keppler, Julia K., Timon R. Heyn, Jacqueline Lux, Therese Ruhmlieb, Laura Meissner, Loes J. G. Hoppenreijs, Anja Steffen-Heins, and Karin Schwarz. "(Amyloid) Protein Aggregates from β-Lactoglobulin and Their Behavior Along the Process Chain." In Dispersity, Structure and Phase Changes of Proteins and Bio Agglomerates in Biotechnological Processes, 201–39. Cham: Springer Nature Switzerland, 2024. http://dx.doi.org/10.1007/978-3-031-63164-1_7.

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Conference papers on the topic "Β-amyloid structures"

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Park, Jiyong, Byungnam Kahng, and Wonmuk Hwang. "Supramolecular Structure and Stability of the GNNQQNY β-Sheet Bilayer Filament: A Computational Study." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-175588.

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Self-assembly of β-sheet forming peptides into filaments has drawn great interests in biomedical applications [1,2]; Hydrogels formed by filaments self-assembled from de novo designed peptides possess potential applications for cell culture scaffolds [3]. On the other hand, peptides derived from amyloidogenic proteins in neurodegenerative diseases such as Alzheimer’s and Parkinson’s also form similar β-sheet filaments in vitro. They share little sequence homology, yet filaments formed by these self-assembling peptides commonly have the cross-β structure, the key signature of the amyloid fibril. Detailed structural information of the self-assembled β-sheet filaments has been limited partly due to the difficulty in preparing ordered filament samples, and it has been only recently that solid-state nuclear magnetic resonance and x-ray techniques have revealed their molecular structure at the atomic level [4,5]. Although molecular structures of amyloid fibrils are becoming available, physical principles governing their self-assembly and the properties of the filaments are not well-understood, for which computational as well as theoretical approaches are desirable [6].

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Athamneh, Ahmad, and Justin Barone. "Enzyme-Mediated Self-Assembly of Highly Ordered Structures From Disordered Proteins." In ASME 2008 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. ASMEDC, 2008. http://dx.doi.org/10.1115/smasis2008-540.

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Trypsin hydrolysis of wheat gluten produced glutamine-rich short peptides with a tendency to self-assemble into supermolecular structures extrinsic to native wheat gluten. Fourier transform infrared and X-ray diffraction data suggested that the new structures formed resembled that of cross-β amyloid fibrils found in some insect silk and implicated in prion diseases. The superstructures were about 10 μm in diameter with clear right-handed helical configuration and appeared to be bundles of smaller fibrils of about 63 nm in diameter. Results demonstrate the potential for utilizing cheap protein sources and natural mechanisms of protein self-assembly to design advanced nanomaterials that can provide a wide range of structural and chemical functionality.

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Shutikov, A. A., G. M. Arzumanyan, K. Z. Mamatkulov, E. Arynbek, and D. S. Zakrytnaya. "ANALYSIS OF THE SECONDARY STRUCTURE OF AΒ (1-42) PEPTIDE IN THE AMIDE I REGION BY RAMAN SPECTROSCOPY." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-220.

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Amyloid fibrils found in plaques in Alzheimer’s disease (AD) brains are composed of amyloid-β peptides. Aβ peptides are formed from the transmembrane amyloid precursor protein (APP). They have pronounced fibrillogenic properties, and its oligomers are toxic to nerve cells, causing their degeneration and death. Oligomeric amyloid-β (1-42) is thought to play a critical role in neurodegeneration in AD. In this work, we analyzed the conformational transformation of Aβ (1-42) peptides embedded in membrane mimetics by Raman spectroscopy. The main goal of the scientific study was to investigate the structural changes of the peptide leading to the formation of amyloid oligomers and fibrils.

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Souza, Giordana S., Samara O. Pinto, and Ana Maria Marques da Silva. "Evaluation of MR-less in brain amyloid-β PET Centiloid quantification." In Biomedical Applications in Molecular, Structural, and Functional Imaging, edited by Barjor S. Gimi and Andrzej Krol. SPIE, 2022. http://dx.doi.org/10.1117/12.2611904.

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Lomakin, Aleksey, David B. Teplow, Daniel A. Kirschner, and George B. Benedek. "Nucleation and Growth of Amyloid β-Protein Fibrils: Detection of Nuclei and Quantitation of Rate Constants." In Photon Correlation and Scattering. Washington, D.C.: Optica Publishing Group, 1996. http://dx.doi.org/10.1364/pcs.1996.sab.3.

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Alzheimer's disease is a progressive, neurodegenerative disorder characterized by amyloid deposition in senile plaques in the cerebral parenchyma and vasculature.(1) These plaques are composed primarily of fibers of the amyloid β-protein, Aβ. A number of studies have provided information on the structure of fibrils formed both in vivo and in vitro, and on factors affecting fiber formation. Synthetic Aβ peptides also form fibers which are ultrastructurally indistinguishable from those isolated from the brain. These peptides have been utilized to examine how a variety of parameters, including temperature, pH, solvent composition, peptide concentration, and peptide sequence, influence the final structure of Aβ aggregates. What is substantially less understood, however, is the kinetics of Aβ fibril growth.

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Silva, Letícia Freitas de Castro, Elisa Pinheiro Weber, Gleice Silva Toledo, and Josiane Fonseca Almeida. "New pharmacological strategies for the treatment of alzheimer’s disease." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.097.

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Introduction: Alzheimer’s disease (AD) is seen as the most important dementia, prevalent in the elderly over 60 years old. There is still no cure, and the pharmacological strategies are to delay the symptoms and development of the pathology. The pathophysiological mechanisms are: hyperphosphorylation of the tau protein and aggregation of amyloid-β. Update studies of the tested therapies target the main pathological mechanisms: accumulation of β amyloid (inhibitors and modulators of β-secretase and γ-secretase and active and passive anti-Aβ immunotherapies), tau protein (inhibition of abnormal hyperphosphorylation with GSK-3 inhibitors, passive and active immunotherapies and the use of intrathecal antisense oligonucleotides (ASOs) and correction of the ApoE protein (increase lipidation, correct structure, clearance of non-lipid ApoE and reduction of ApoE expression). Objectives and methodology: To develop a bibliographic review in order to address new drugs in the treatment of Alzheimer’s. Qualitative and descriptive study carried out by literary review with research on PubMed. Results: Several drugs have been tested in clinical trials, however, due to lack of effectiveness, none have been approved. Therefore, it’s important to understand the limitations of the tests developed as flaws in the methodology, insufficient understanding of the mechanisms involved and inclusion of patients in different stages of AD, so that future investigations can overcome these gaps. Conclusion: It’s important to investigate new pathophysiological mechanisms, as well as the factors that trigger AD. Diagnosis is essential, with further studies to identify new biomarkers of the disease that will also have an impact on the conduct of clinical trials.

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Chiu, K. C., L. Y. Yu, J. N. Yih, and S. J. Chen. "Investigating the structural changes of β-amyloid peptide aggregation using attenuated-total-reflection surface-enhanced Raman spectroscopy." In Biomedical Optics (BiOS) 2007, edited by Tuan Vo-Dinh and Joseph R. Lakowicz. SPIE, 2007. http://dx.doi.org/10.1117/12.701757.

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"818 BGRS/SB-2022 The low-molecular-weight ligands of human serum albumin, promoting its interaction with amyloid β peptide." 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-2022-475.

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"All-D-enantiomeric peptide designed for Alzheimer´s disease treatment dynamically interacts with amyloidogenic region of membrane-bound amyloid-β peptide precursor." 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-2022-175.

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"BGRS/SB-2022 779 In search for the peptide/protein ligands of human serum albumin able to affect its interaction with amyloid β peptide." 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-2022-449.

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Reports on the topic "Β-amyloid structures"

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Wing Hei Cheng, Cecily, Matthew Hai Heng Chung, and Joseph Chi Fung Ng. Structural Dynamics of Amyloid-β Aggregation in Alzheimer’s Disease: Computational and Experimental Approaches. Journal of Young Investigators, December 2016. http://dx.doi.org/10.22186/jyi.31.6.44-50.

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Zhang, Yu, Chaoliang Sun, Hengxi Xu, Weiyang Shi, Luqi Cheng, Alain Dagher, Yuanchao Zhang, and Tianzi Jiang. Connectivity-Based Subtyping of De Novo Parkinson Disease: Biomarkers, Medication Effects and Longitudinal Progression. Progress in Neurobiology, April 2024. http://dx.doi.org/10.60124/j.pneuro.2024.10.04.

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Parkinson's disease (PD) is characterized by divergent clinical symptoms and prognosis, suggesting the presence of distinct subtypes. Identifying these subtypes is crucial for understanding the underlying pathophysiology, predicting disease progression, and developing personalized treatments. In this study, we propose a connectivity-based subtyping approach, which measures each patient's deviation from the reference structural covariance networks established in healthy controls. Using data from the Parkinson's Progression Markers Initiative, we identified two distinct subtypes of de novo PD patients: 248 patients with typical cortical-striato-thalamic dysfunctions and 41 patients showing weakened dorsal raphe nucleus (DRN)-to-cortical/striatal projections. The proposed subtyping approach demonstrated high stability in terms of random sampling of healthy or diseased population and longitudinal prediction at follow-up visits, outperforming the traditional motor phenotypes. Compared to the typical PD, patients with the DRN-predominant subtype were characterized by less server motor symptoms at baseline and distinct imaging biomarkers, including larger striatal volumes, higher concentration of cerebrospinal fluid amyloid-β and amyloid-β/t(p)-tau ratio. Subtype-specific associations and drug effects were identified that the DRN subtype exhibited more pronounced medication effects on motor symptoms, potentially regulated by DRN serotonergic modulation through striatal dopaminergic neurons. The DRN serotonergic inputs also regulated non-motor symptoms, the aggregation of CSF biomarkers and the conversion to more severe disease states. Our findings suggest that the DRN-predominant subtype represents a unique clinical and biological phenotype of PD characterized by an enhanced response to anti-parkinsonian treatment, more favorable prognosis and slower progression of dopamine depletion. This study may contribute to clinical practice of precision medicine, early invention and individualized treatments in PD and other neurodegenerative diseases.

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