Titre : |
Modulation of Alzheimer's disease amyloid beta peptide aggregation by molecular chaperones, polyphosphates and metal ions, and their interplay |
Type de document : |
texte imprimé |
Auteurs : |
Sara Maria Ayala Mariscal, Auteur ; Pierre Genevaux, Directeur de thèse ; Hureau, Christelle, Directeur de thèse |
Langues : |
Anglais (eng) |
Tags : |
ALZHEIMER’S AMYLOID BETA MOLECULAR CHAPERONES AGGREGATION POLYPHOSPHATES ZINC COPPER |
Résumé : |
"Alzheimer's disease is the most frequent type of dementia. With an exponentially growing number of cases, understanding the underlying molecular events leading to this devastating condition is of crucial importance. Much evidence points to a disequilibrium in the production and degradation of amyloid beta (Aß), a normally physiological 42 amino acid peptide, as an early key event in Alzheimer's etiology. Whether Aß is overproduced or poorly degraded, the overall result is an abnormally large pool of peptide that gradually aggregates forming extracellular deposits of fibrils, called amyloid plaques, in specific brain regions. Hence, modulation of Aß aggregation process is one of the suggested approaches to control the evolution of Alzheimer's disease. Universally conserved molecular chaperones have been intensively studied for their capacity to prevent aggregation of disease-related proteins, and many of them have proven to efficiently modulate Alzheimer's Aß aggregation. In a scenario where chaperones are overexpressed or directly administered into the affected tissue, the universal conservation and the relatively poor client-specificity of generic chaperones can become a downside because of the risk of interaction with proteins other than the targeted one is not dismissible, and thus the consequences unpredictable. In the first part of this work, we looked upon a bacterial chaperone call SecB with an unusually robust holdase activity (i.e. it prevents early protein folding) as a promising modulator of Alzheimer's Aß peptide aggregation. [...]" |
Document : |
Thèse de Doctorat |
Etablissement_delivrance : |
Université Toulouse 3 |
Date_soutenance : |
12/01/2018 |
Ecole_doctorale : |
Sciences de la matière (SdM) |
Domaine : |
Chimie, Biologie, Santé |
En ligne : |
http://thesesups.ups-tlse.fr/4344/ |
Modulation of Alzheimer's disease amyloid beta peptide aggregation by molecular chaperones, polyphosphates and metal ions, and their interplay [texte imprimé] / Sara Maria Ayala Mariscal, Auteur ; Pierre Genevaux, Directeur de thèse ; Hureau, Christelle, Directeur de thèse . - [s.d.]. Langues : Anglais ( eng)
Tags : |
ALZHEIMER’S AMYLOID BETA MOLECULAR CHAPERONES AGGREGATION POLYPHOSPHATES ZINC COPPER |
Résumé : |
"Alzheimer's disease is the most frequent type of dementia. With an exponentially growing number of cases, understanding the underlying molecular events leading to this devastating condition is of crucial importance. Much evidence points to a disequilibrium in the production and degradation of amyloid beta (Aß), a normally physiological 42 amino acid peptide, as an early key event in Alzheimer's etiology. Whether Aß is overproduced or poorly degraded, the overall result is an abnormally large pool of peptide that gradually aggregates forming extracellular deposits of fibrils, called amyloid plaques, in specific brain regions. Hence, modulation of Aß aggregation process is one of the suggested approaches to control the evolution of Alzheimer's disease. Universally conserved molecular chaperones have been intensively studied for their capacity to prevent aggregation of disease-related proteins, and many of them have proven to efficiently modulate Alzheimer's Aß aggregation. In a scenario where chaperones are overexpressed or directly administered into the affected tissue, the universal conservation and the relatively poor client-specificity of generic chaperones can become a downside because of the risk of interaction with proteins other than the targeted one is not dismissible, and thus the consequences unpredictable. In the first part of this work, we looked upon a bacterial chaperone call SecB with an unusually robust holdase activity (i.e. it prevents early protein folding) as a promising modulator of Alzheimer's Aß peptide aggregation. [...]" |
Document : |
Thèse de Doctorat |
Etablissement_delivrance : |
Université Toulouse 3 |
Date_soutenance : |
12/01/2018 |
Ecole_doctorale : |
Sciences de la matière (SdM) |
Domaine : |
Chimie, Biologie, Santé |
En ligne : |
http://thesesups.ups-tlse.fr/4344/ |
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