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Dissertations / Theses on the topic 'Interactions peptides amyloides'

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Published: 4 June 2021

Last updated: 10 February 2022

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1

Lambert, Eléonore. "Apports de la Microscopie à Force Atomique à l’étude de phénomènes dynamiques en biologie et développement instrumental associé." Thesis, Reims, 2018. http://www.theses.fr/2018REIMS014/document.

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Le Laboratoire de Recherche en Nanosciences EA 4682 s’est récemment équipé de la microscopie à force atomique haute-vitesse (HS-AFM) permettant la visualisation en temps réel des dynamiques d’interactions d’un panel infini d’échantillons biologiques à l’échelle nanométrique. De nombreux champ de recherche nécessite la mise au point de techniques permettant à la fois une imagerie dynamique (vidéomicroscopie) mais également de plus en plus une imagerie haute résolution (microscopie champ proche). Ce couplage a été récemment obtenu grâce au développement de la microscopie à force atomique ultra-r

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2

Hornshaw, Martin P. "Peptide metal ion interactions in cerebral amyloidoses." Thesis, University of Newcastle Upon Tyne, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.260931.

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3

Chouchane, Karim. "Contrôler l'agrégation de l'insuline à la surface des matériaux via des interactions avec des peptides et la lumière." Thesis, Université Grenoble Alpes (ComUE), 2017. http://www.theses.fr/2017GREAY072/document.

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Le repliement et la stabilité des protéines dépendent des conditions physico-chimiques de leur environnement. En particulier, le pH, la température, l’agitation et les interactions avec d’autres macromolécules ou avec les interfaces (liquide–surfaces des matériaux ; air-liquide ; etc.) sont connues pour induire des phénomènes de dénaturation et d’agrégation des protéines.Le contrôle de la stabilité des protéines thérapeutiques représente un enjeu médical et économique pour l’industrie pharmaceutique. L’insuline, qui est la protéine thérapeutique la plus produite, est connue in vitro pour forme

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4

Bell, Leonard Gerald. "Interactions between #beta#-amyloid peptide and metal ions in amyloid formation." Thesis, University of Sunderland, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337181.

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5

Zhang, Mingzhen. "Multiscale Molecular Simulations of Cross-sequence Interactions between Amyloid Peptides." University of Akron / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=akron1490711960550386.

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6

Ma, Xin. "The interaction between amyloid beta peptide and phospholipids." Thesis, University of Edinburgh, 2015. http://hdl.handle.net/1842/29637.

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The aim of the thesis project was to examine what form(s) of Amyloid beta (Aβ) (25-‐35) peptide interact with phospholipids in vitro and the implications of this for the mechanism of Alzheimer’s Diseases (AD). The mechanism of AD is thought to involve protein folding and misfolding. An increasing amount of evidence has shown that protein misfolding plays an important role in the biological and pathological processes of AD. Although seen as the biomedical markers of those diseases, the roles of amyloid aggregates themselves are still not fully understood. Whether the aggregates, or the monomer

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7

Widenbrant, Martin Johan Olof. "Investigation of amyloid-beta peptide interactions with membrane lipids /." May be available electronically:, 2007. http://proquest.umi.com/login?COPT=REJTPTU1MTUmSU5UPTAmVkVSPTI=&clientId=12498.

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8

Turner, Matthew. "Modelling platinum(II) interactions with the Amyloid-b peptide." Thesis, Cardiff University, 2018. http://orca.cf.ac.uk/109924/.

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The Ab peptide is a key molecule in the development of Alzheimer’s Disease - Ab peptides form toxic aggregates in the brain. Density functional theory (DFT), Parametric Model 7 (PM7) and ligand-Field Molecular Mechanics (LFMM) methods have been used to model the interactions of a series of potential therapeutic PtII(ligand) complexes with various fragments of the Ab peptide. LFMM calculations with the AMBER forcefield were used to generate conformations of PtII-Ab6-14 via LowMode MD and results validated against BHandH. While LFMM showed insufficient agreement with DFT, the semi-empirical PM7

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9

Kamaloo, Elaheh. "Supported lipid bilayer interactions with nanoparticles, peptides and polymers." Digital WPI, 2018. https://digitalcommons.wpi.edu/etd-dissertations/38.

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Supported lipid bilayers (SLBs) are one of the most common model membranes used in the field of cell membrane biology as they provide a well-defined model membrane platform for determination of molecular-level interactions between different biomolecules (e.g. proteins, peptides) and lipid membrane. Compared to model organisms, the use of SLB is preferable since it mimics cell plasma membrane in a very simple and well-controlled way. Therefore, molecular structure of membrane and experimental conditions (e.g. solution chemistry, temperature, and pH) can be easily adjusted to the required condi

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10

Senyah, Nancy Akosuah. "The interactions of Alzheimer's amyloid peptides with artificial and biological membranes." Thesis, University of Essex, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.284610.

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11

Hoffmann, Anais. "Oligomerization and fibrillization properties of amyloid peptides and interactions with inhibitors." Thesis, Paris 6, 2015. http://www.theses.fr/2015PA066442/document.

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Les maladies amyloïdes sont des affections sévères caractérisées par la présence de dépôts extracellulaires fibreux susceptibles de toucher un ou plusieurs tissus du corps humain. Au cours de ma thèse, je me suis intéressée au peptide β amyloïde (Aβ), impliqué dans la maladie d’Alzheimer, ainsi que l’amyline ou Islet Amyloid PolyPeptide (IAPP), impliqué dans le diabète de type 2. Le mécanisme de formation des fibres a été décrit comme un processus en deux étapes : la nucléation, conduisant à la formation d’oligomères et la phase d’élongation conduisant à la formation des fibres. La première pa

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12

Vahdati, Leïla. "Synthesis of peptidomimetics containing bifunctional diketoopiperazine scaffolds and their evaluation as modulators of amyloid-B peptide oligomerization." Thesis, Paris 11, 2015. http://www.theses.fr/2015PA114811/document.

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La formation des agrégats des peptides et des protéines par l'interaction de feuillets β a de plus en plus attiré l'attention car elle se produit dans de nombreuses maladies humaines généralisées, telles que la sclérose latérale amyotrophique (SLA), la maladie d'Alzheimer (AD), la maladie de Parkinson (PD), les maladies à prions et la maladie de Huntington (HD). La maladie d'Alzheimer est la forme la plus courante de démence qui provoque la perte de la mémoire chez les personnes âgées. En 2013, il y avait 35 millions de personnes souffrant de AD à travers le monde, un chiffre qui devrait doubl

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13

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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14

Danielsson, Jens. "NMR studies of the amyloid beta-peptide." Doctoral thesis, Stockholm University, Department of Biochemistry and Biophysics, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1410.

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<p>The Amyloid beta peptide (Ab) is related to Alzheimer’s disease and is suggested to be the molecular pathogenic species of the disease, probably through the neurotoxic effect of Ab oligomers. Here the results from biophysical studies of Ab and fragments thereof, are presented. Pulsed field gradient NMR diffusion experiments show that Ab exists mainly as an unfolded monomer. In addition, the hydrodynamic radius of Ab suggests that Ab has residual secondary structure propensities. CD experiments reveal that Ab has a high propensity to adopt a polyproline type II (PII) helix at low temperature

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15

Österlund, Nicklas. "Gas phase studies of the Amyloid-β peptide : Peptide oligomerization and interactions with membrane mimetics". Thesis, Stockholms universitet, Institutionen för biokemi och biofysik, 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-155009.

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The amyloid-β peptide is an amphiphilic peptide that exhibits self-aggregating properties, forming the amyloid fibrils that can be found in the brains of Alzheimer patients. Today it is believed that it is the soluble Aβ oligomers rather than the mature fibrils that are the main neurotoxic species. These small peptide assemblies are known to associate with lipid membranes and form pores that can transport Ca2+ into the cell, which in part could be responsible for their neurotoxic properties. However, most biophysical methods that have been developed to study Aβ target either the monomer or the

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16

Saurabh, Rahul. "Interaction between the Alzheimer's peptide, beta-amyloid and lipid membrane." Thesis, University of Hull, 2015. http://hydra.hull.ac.uk/resources/hull:13635.

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Alzheimer’s disease (AD) is a neurodegenerative disorder. The patho-physiological effects of amyloid beta (Aβ) may be mediated by Aβ-membrane interaction. However, the molecular mechanism of interaction between Aβ and neuronal membrane remains unknown. The aim of the study was to investigate the interaction of a toxic fragment of amyloid beta, Aβ₂₅-₃₅ with the lipid membrane model using model lipid bilayers and beta breaker peptide, KLVFF. Liquid ¹H NMR assay was used to investigate the aggregation properties of Aβ₂₅-₃₅. The sharp NMR peaks of Aβ₂₅-₃₅ appeared immediately after sample preparat

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17

Hu, Rundong. "CROSS-INTERACTION AND INHIBITION OF AMYLOID POLYPEPTIDE AGGREGATION." University of Akron / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=akron1490383234134397.

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18

Wahlström, Anna. "NMR studies on interactions between the amyloid β peptide and selected molecules". Doctoral thesis, Stockholms universitet, Institutionen för biokemi och biofysik, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-60346.

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Alzheimer’s disease is an incurable neurodegenerative disorder linked to the amyloid β (Aβ) peptide, a 38-43 residue peptide. The detailed molecular disease mechanism(s) is (are) unknown, but oligomeric Aβ structures are proposed to be involved. In common for the papers in this thesis is interactions; interactions between Aβ(1-40) and selected molecules and metal ions. The purpose has been to find out more about the structural states that Aβ can adopt, in particular the β-sheet state, which probably is linked to the oligomeric structures. The methods used have been nuclear magnetic resonance (

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19

Martineau, Eric. "Modeling Peptide-binding Interactions and Polymer-binding Interactions and their Role in Mass Spectrometry." Thèse, Université d'Ottawa / University of Ottawa, 2013. http://hdl.handle.net/10393/24197.

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As a first project, collision-induced dissociation experiments were carried out using electrospray ionisation mass spectrometry on gas phase complexes involving different poly(methylmetacrylate) oligomers with three amino acids: glycine, leucine, and phenylalanine. After acquiring breakdown diagrams, RRKM modeling was used to fit the experimental data in order to obtain the 0 K activation energy and the entropy of activation. These thermodynamic data were then used to understand the competing dissociation channels observed (except for gas phase complexes involving glycine that had only one dis

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20

Maltseva, Elena. "Model membrane interactions with ions and peptides at the air,water interface." Phd thesis, [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=976724537.

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21

Brown, Anne M. "Insights into Mechanisms of Amyloid Toxicity: Molecular Dynamics Simulations of the Amyloid andbeta-peptide (Aandbeta) and Islet Amyloid Polypeptide (IAPP)." Diss., Virginia Tech, 2016. http://hdl.handle.net/10919/73773.

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Aggregation of proteins into amyloid deposits is a common feature among dozens of diseases. Two such diseases that feature amyloid deposits are Alzheimer's disease (AD) and type 2 diabetes (T2D). AD toxicity has been associated with the aggregation and accumulation of the amyloid β-peptide (Aβ); Aβ exerts its toxic effects through interactions with neuronal cell membranes. A characteristic feature of T2D is the deposition of the islet amyloid polypeptide (IAPP) in the pancreatic islets of Langerhans. It is currently unknown if IAPP aggregation is a cause or consequence of T2D, but it does lead

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22

Braun, Sebastian. "Mutual interactions of basic peptides with nucleic and fatty acids : amyloid nucleation, membrane disruption, and hybridisation." Thesis, Cardiff University, 2013. http://orca.cf.ac.uk/46189/.

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Anions including nucleic acids and lipids have been found to promote amyloid formation in diseases including neurodegenerative conditions such as Alzheimer’s and Creutzfeldt-Jakob disease. However, the direct effects of these close charge-based interactions are not well understood. It is unclear what effect amyloidogenic peptides would have on nucleic acid integrity. Similarly, the direct effects of amyloidogenic polypeptides on liposomes are not well understood. Here I have used a simplified system of short basic peptides with alternating hydrophobic and hydrophilic amino acid residues to stu

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23

Wang, Feng. "Interaction between pancreatic cancer and beta cells : intraislet significance of islet amyloid polypeptide /." Stockholm, 1998. http://diss.kib.ki.se/1998/91-628-3300-6/.

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24

Hugonin, Loïc. "Spectroscopic studies of dynorphin neuropeptides and the amyloid beta-peptide : The consequences of biomembrane interactions." Doctoral thesis, Stockholm University, Department of Biochemistry and Biophysics, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-7156.

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<p>Dynorphin A, dynorphin B and big dynorphin are endogenous opioid neuropeptides. They play an important role in a wide variety of physiological functions such as regulation of pain processing and memory acquisition. Such actions are generally mediated through the κ-receptors. Besides opioid receptor interactions, dynorphins have non-opioid physiological activities which result in excitotoxic effects in neuropathic pain, spinal cord and brain injury. In order to gain insight into the mechanisms of the non-opioid interactions of dynorphins with the cell, spectroscopic membrane-interaction stud

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25

Hugonin, Loïc. "Spectroscopic studies of dynorphin neuropeptides and the amyloid beta-peptide : the consequences of biomembrane interactions /." Stockholm : Department of Biochemistry and Biophysics, Stockholm university, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-7156.

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26

Maftei, Madalina [Verfasser]. "Molecular characterization of neuroprotective β-amyloid interacting peptides and autoantibodies relevant to Alzheimer’s disease / Madalina Maftei". Konstanz : Bibliothek der Universität Konstanz, 2015. http://d-nb.info/1081016914/34.

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27

Gilson, Virginie. "Interaction du peptide beta amyloïde avec les membranes plasmiques cellulaires." Thesis, Strasbourg, 2013. http://www.theses.fr/2013STRAJ020/document.

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La maladie d’Alzheimer (MA) est une maladie neurodégénérative du système nerveux central qui se caractérise notamment par l’accumulation de peptide beta-amyloïde (Aβ) dans le tissus nerveux. Dans la première partie de cette thèse nous avons montré que l’interaction des oligomères Aβ1-42 de haut poids moléculaire avec la membrane plasmique des cellules PC12 différenciées ou des cellules nerveuses (neurones et astrocytes primaires) provoque des variations de la [Ca2+]i dépendant de l’activation des récepteurs NMDA. Dans la seconde partie nous avons montré qu’une pré-exposition des cellules PC12

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28

Mari, Meropi. "Investigating the aggregation of β-amyloid peptide (Aβ₄₂) and its interactions with lipid bilayers using advanced microscopy techniques". Thesis, University of Edinburgh, 2014. http://hdl.handle.net/1842/8889.

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The cell membrane is a highly complex structure consisting of a large diversity of phospholipids and macromolecules. There exist a variety of diseases that compromise the integrity of this key component of the cell. This thesis considers the investigation of interactions between β-amyloid peptide (Aβ₄₂) and lipid bilayers. To facilitate understanding of this complex system, it is advantageous to employ a model sample; supported lipid bilayers (SLB) and giant multilamellar vesicles (MLVs) are used as proxy cell membranes. These nanostructures are widely used as models of cellular membranes in m

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29

Lemkul, Justin Alan. "Molecular Modeling of the Amyloid β-Peptide: Understanding the Mechanism of Alzheimer's Disease and the Potential for Therapeutic Intervention". Diss., Virginia Tech, 2012. http://hdl.handle.net/10919/77318.

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Alzheimer's disease is the leading cause of senile dementia in the elderly, and as life expectancy increases across the globe, incidence of the disease is continually increasing. Current estimates place the number of cases at 25-30 million worldwide, with more than 5.4 million of these occurring in the United States. While the exact cause of the disease remains a mystery, it has become clear that the amyloid β-peptide (Aβ) is central to disease pathogenesis. The aggregation and deposition of this peptide in the brain is known to give rise to the hallmark lesions associated with Alzheimer's dis

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30

Prade, Elke [Verfasser], Bernd [Akademischer Betreuer] Reif, Bernd [Gutachter] Reif, and Aphrodite [Gutachter] Kapurniotu. "Structural Characterization of Interactions between the Alzheimer’s Disease Amyloid-Beta Peptide and Small Molecules and Peptide Inhibitors / Elke Prade ; Gutachter: Bernd Reif, Aphrodite Kapurniotu ; Betreuer: Bernd Reif." München : Universitätsbibliothek der TU München, 2015. http://d-nb.info/1149252227/34.

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31

Padayachee, Eden Rebecca. "Neuronal nitric oxide synthase : a biomarker for Alzheimers disease : interaction of neuronal nitric oxide synthase with beta-amyloid peptides in the brain." Thesis, Rhodes University, 2011. http://hdl.handle.net/10962/d1007677.

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High levels of the amino acid arginine and low levels of the product citrulline in the cerebrospinal fluid of Alzheimer's patients could mean that there is a decrease in the enzymes that metabolize this amino acid. One such enzyme is neuronal nitric oxide synthase (nNOS). In this study, neuronal nitric oxide synthase (nNOS), sourced from bovine brain was extracted and concentrated using two methods of precipitation: poly (ethylene glycol) 20 000 (PEG) and ammonium sulphate [(NH₄)₂S0₄). These two techniques gave no increase in yield nor fold purification and hence were abandoned in favour of io

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32

Li, Xiaoman. "Study on memapsin 2 cleavage properties and its interacting proteins." Oklahoma City : [s.n.], 2010.

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33

Henry, Sarah. "Interaction du peptide Aβ1-42 et mutants avec des membranes modèles : de l'échelle micrométrique à l'échelle nanométrique". Thesis, Bordeaux, 2015. http://www.theses.fr/2015BORD0159/document.

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La maladie d'Alzheimer, maladie neurodégénérative la plus courante, est la cause de50% des cas de démence. La maladie d’Alzheimer est provoquée par l'agrégation d'unamyloïde, le peptide Aβ1-42, dans le cerveau des patients.De nombreuses études relient la toxicité des amyloïdes à l'existence de diversesstructures intermédiaires survenant avant la formation des fibres et / ou leur interactionspécifique avec les membranes.Dans cette étude, nous nous sommes centrés sur l'interaction entre des modèlesmembranaires et le peptide Aβ1-42 (WT et des mutants plus ou moins toxiques) évaluée parplusieurs t

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34

Poojari, Chetan Verfasser], Birgit [Akademischer Betreuer] Strodel, and Dieter [Akademischer Betreuer] [Willbold. "Interaction of amyloid peptides with biomembranes and its implications in Alzheimers disease and type II diabetes / Chetan Poojari. Gutachter: Birgit Strodel ; Dieter Willbold." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2013. http://d-nb.info/1042276013/34.

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35

Younan, Nadine D. "The influence of copper (II) ions on the structure and stability of the prion protein and its interaction with the amyloid-beta peptides." Thesis, Queen Mary, University of London, 2012. http://qmro.qmul.ac.uk/xmlui/handle/123456789/2510.

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The prion protein (PrPC) is a cell surface glycoprotein that binds Cu2+ ions. The misfolding and oligomerisation of PrPC is responsible for a range of transmissible spongiform encephalopathies (TSEs) in mammals. As changes in PrPC conformation are intimately linked with disease pathogenesis, the effect of Cu2+ ions on the structure and stability of PrPC has been investigated. In chapter 3, urea unfolding studies indicate that Cu2+ ions destabilise the native fold of PrPC. The mid-point of the unfolding transition is reduced by 0.73 ± 0.05 M urea in the presence of Cu2+ ions equating to an appr

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36

Poojari, Chetan [Verfasser], Birgit Akademischer Betreuer] Strodel, and Dieter [Akademischer Betreuer] [Willbold. "Interaction of amyloid peptides with biomembranes and its implications in Alzheimers disease and type II diabetes / Chetan Poojari. Gutachter: Birgit Strodel ; Dieter Willbold." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2013. http://d-nb.info/1042276013/34.

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37

Bokvist, Marcus. "Membrane mediated aggregation of amyloid-β protein : a potential key event in Alzheimer's disease". Doctoral thesis, Umeå universitet, Kemi, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-969.

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The pathogenesis of Alzheimer’s disease (AD), the most common senile dementia, is a complex process. A crucial event in AD is the aggregation of amyloid-β protein (Aβ), a cleavage product from the Amyloid Precursor Protein (APP). Aβ40, a common component in amyloid plaques found in patients, aggregates in vitro at concentrations, much higher than the one found in vivo. But in the presence of charged lipid membranes, aggregations occurs at much lower concentration in vitro compared to the membrane-free case. This can be understood due to the ability of Aβ to get electrostatically attracted to t

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38

Djogo, Nevena [Verfasser], та MELITTA [Akademischer Betreuer] SCHACHNER. "The interaction between the neural cell adhesion molecule L1 and β-amyloid peptide : potential relevance in Alzheimer’s disease / Nevena Djogo. Betreuer: Melitta Schachner". Hamburg : Staats- und Universitätsbibliothek Hamburg, 2013. http://d-nb.info/1045730440/34.

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Jin, Sha. "Membrane interaction of amyloid–beta (1–42) peptide induces membrane remodeling and benefits the conversion of non–toxic Aβ species into cytotoxic aggregate". Doctoral thesis, Humboldt-Universität zu Berlin, Lebenswissenschaftliche Fakultät, 2016. http://dx.doi.org/10.18452/17632.

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Das Amyloid-beta Peptid (Ab) ist der Hauptbestandteil der extrazellulären Plaques bei der Alzheimerschen Krankheit. Das Ziel der vorliegenden Arbeit ist es, die Mechanismen der Wechselwirkungen des Ab mit der Plasmamembran und der nachfolgenden zellulären Aufnahme aufzuklären. Die Aggregation, die zelluläre Aufnahme und die Zytotoxizität von Ab42 wurden durch Verwendung von fluoreszenzmarkierten Ab42 in einem Neuroblastomzellkulturmodell untersucht. Sowohl bei Inkubation mit Monomeren als auch mit Aggregaten wurde in den Zellen Ab42 detektiert. Dabei binden Ab42 Monomere und kleine Aggregate z

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40

Lindström, Fredrick. "Biological membrane interfaces involved in diseases : a biophysical study." Doctoral thesis, Umeå universitet, Kemi, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-806.

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Interactions between peptides and biological lipid membranes play a crucial role in many cellular processes such as in the mechanism behind Alzheimer’s disease where amyloid-beta peptide (Abeta)is thought to be a key component. The initial step of binding between a surface active peptide and its target membrane or membrane receptor can involve a non specific electrostatic association where positively charged amino acid residues and a negatively charged membrane surface interact. Here, the use of high resolution MAS NMR provides a highly sensitive and non perturbing way of studying the electros

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41

Kihal, Nadjib. "Synthèse et évaluation pharmacologique de nouveaux peptides biomimétiques et de benzothiadiazines." Phd thesis, Université Paris Sud - Paris XI, 2013. http://tel.archives-ouvertes.fr/tel-00940587.

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Les canaux potassiques sensibles à l'ATP (KATP) jouent un rôle primordial dans plusieurs processus cellulaires. La modulation de ces canaux par des molécules activatrices constituerait des applications pharmacologiques et médicinales très intéressantes. À cet effet nous avons conçu et synthétisé de nouvelles molécules hybrides cromakalim-diazoxide et diazoxide-amine/aminoacide. Nous avons également, évalué l'activité myorelaxante de ces composés sur l'aorte de rates. Les résultats obtenus ne montrent pas un effet myorelaxant significatif. Des études sur d'autres tissus, notamment les cellules

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Andreetto, Erika [Verfasser], Aphrodite Akademischer Betreuer] Kapurniotu та Horst [Akademischer Betreuer] [Kessler. "Identification of sequences of the interaction interface of β-amyloid peptide (Aβ) and islet amyloid polypeptide (IAPP) and synthesis and characterization of IAPP-derived inhibitors of Aβ aggregation / Erika Andreetto. Gutachter: Horst Kessler ; Aphrodite Kapurniotu. Betreuer: Aphrodite Kapurniotu". München : Universitätsbibliothek der TU München, 2011. http://d-nb.info/1056936630/34.

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43

Mohammadi, Azadeh. "Apolipoprotein E isoform specific differences on their tertiary structure and on their interaction with amyloid-β peptide: Structural and dynamics studies by cross-linking mass spectrometry and in silico modeling". Doctoral thesis, Universite Libre de Bruxelles, 2017. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/257269.

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La maladie d’Alzheimer (MA) est un désordre neuro-dégénératif chronique fatal et la forme la plus répandue des démences chez l’adulte qui touchent plus de 28 millions de personnes dans le monde. En absence de traitement pour les démences neurodégénérative dont la maladie d’Alzheimer, le coût de celles-ci est estimé à 1 trillion d’USD en 2018 ce qui représente des enjeux économiques et sociétaux majeurs au niveau national et mondial. La MA est une forme d’amylose qui est caractérisée par l’agrégation du peptide amyloïde beta (Aβ) dans le cerveau des patients. Le facteur de risque génétique prin

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Palmblad, Magnus. "Identification and Characterization of Peptides and Proteins using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry." Doctoral thesis, Uppsala universitet, Institutionen för materialvetenskap, 2002. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-1999.

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Mass spectrometry has in recent years been established as the standard method for protein identification and characterization in proteomics with excellent intrinsic sensitivity and specificity. Fourier transform ion cyclotron resonance is the mass spectrometric technique that provides the highest resolving power and mass accuracy, increasing the amount of information that can be obtained from complex samples. This thesis concerns how useful information on proteins of interest can be extracted from mass spectrometric data on different levels of protein structure and how to obtain this data expe

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Jin, Sha Verfasser], Erich [Gutachter] [Wanker, Jan [Gutachter] Bieschke та Andreas [Gutachter] Herrmann. "Membrane interaction of amyloid–beta (1–42) peptide induces membrane remodeling and benefits the conversion of non–toxic Aβ species into cytotoxic aggregate / Sha Jin ; Gutachter: Erich Wanker, Jan Bieschke, Andreas Herrmann". Berlin : Lebenswissenschaftliche Fakultät, 2016. http://d-nb.info/1119212049/34.

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Tonali, Nicolo. "Mimes synthétiques de feuillets bêta : conception, synthèse et évaluation de leur capacité à moduler l'agrégation du peptide bêta-amyloïde 1-42." Thesis, Université Paris-Saclay (ComUE), 2016. http://www.theses.fr/2016SACLS544/document.

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La maladie d'Alzheimer (MA) est une maladie neurodégénérative liée à l’oligomérisation et à la fibrillation du peptide bêta amyloïde, avec Abêta 1-42 étant le plus agrégeant et neurotoxique. La cause exacte de la maladie d'Alzheimer n’est pas encore connue et donc il n'y a pas de traitement efficace contre cette maladie.Une stratégie prometteuse pourrait être l'inhibition de l'oligomérisation de monomères solubles d'Abêta;, en stabilisant la conformation non structurée native du peptide, à travers l’utilisation de composés capables d'empêcher la formation de feuillets bêta. En effet, les peu d

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Boehringer, Régis. "Synthèse chimique de protéines pour l'étude structurale et fonctionnelle de fibres amyloïdes." Thesis, Strasbourg, 2018. http://www.theses.fr/2018STRAF001/document.

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Les fibres amyloïdes sont souvent à l’origine de nombreuses maladies dégénératives telles que la maladie d’Alzheimer ou la maladie de Parkinson. La formation de ces plaques insolubles est due à une agrégation anormale de protéines. Les études structurales et biologiques des amyloïdes sont hautement complexes du fait de leur organisation sous forme de superstructures unidirectionnelles composées d’une infinité d’unités peptidiques ou protéiques, mais aussi à cause de leur hétérogénéité conformationnelle et polymorphique. Au cours de ces différents travaux de thèse en collaboration avec différen

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"Interactions of Amyloid-Forming Peptides with Lipid Bilayer Membranes." Thesis, 2012. http://hdl.handle.net/1911/70308.

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Amyloid-proteins are among the most actively researched biological topics today, because they have been associated with many serious human diseases, such as Alzheimer's disease and type II diabetes. In particular the deposition of protein aggregates on cell membranes has been suspected as the causes of the diseases, although the proof is still elusive. Studying the interactions of amyloid-forming peptides with lipid-bilayer membranes may clarify the pathway of the Î²-aggregate formation and provide new insights into the amyloid hypothesis of diseases. In this thesis, I investigate how three pe

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Saraiva, Ana Isabel Lopes Coelho de Mascarenhas. "Interaction studies between biocompatible polymers and amyloid-B peptides." Tese, 2009. http://hdl.handle.net/10216/57913.

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Saraiva, Ana Isabel Lopes Coelho de Mascarenhas. "Interaction studies between biocompatible polymers and amyloid-B peptides." Doctoral thesis, 2009. http://hdl.handle.net/10216/57913.

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