Interactions of metal ions with truncated forms of amyloïd-beta linked to Alzheimer's disease / Aliès, Bruno  

Public ISBD Titre : Interactions of metal ions with truncated forms of amyloïd-beta linked to Alzheimer's disease Type de document : texte imprimé Auteurs : Aliès, Bruno, Auteur ; Faller, Peter, Directeur de thèse ; Hureau, Christelle, Directeur de thèse Année de publication : 2012 Langues : Anglais (eng) Tags : AMYLOID-BETA  AGGREGATION  COORDINATION  METAL IONS  CU  ZN  SPECTROSCOPIES  FLUORESCENCE Résumé : "Amyloid plaques are a hallmark of Alzheimer's disease. These plaques are formed by aggregates of amyloid beta peptides and metal ions. In this context, we studied the interaction of Cu and Zn with the truncated forms of Aß peptides. We focused on two aspect : Coordination and Aggregation. In this first part, we studied coordination of Cu on modified amyloid beta peptide compared to original peptide. These modified peptides are found in human and are considered as more deleterious. Thanks to many spectroscopies (EPR, CD, NMR...), we have shown that (i) pH depending coordination mode of amyloid beta-Cu (ii) the great matter of N-terminal in Cu coordination (iii) the major role of second sphere in coordination (iv) Cu Coordination differences between Aß and his modified forms. In the second part, our aim was to get insights into aggregation mechanisms of peptide modulate by metal ions. Aggregation of peptides is a wide field of interest from neurological diseases to nanotechnology. Thanks to different peptides (from amyloid beta) and several complementary techniques (Fluorescence, Turbitity, TEM...), we have shown that (i) the metal ions coordination dependence of aggregation (ii) acceleration of amyloid beta11-28 aggregation induced by Zn is due to a dimer formation (iii) Changes in Zn coordination induced by pH contribute to slowdown the aggregation (iv) total charge of the dimer determine the precipitation (v) Zn coordination to amyloid beta11-28 is highly dynamic ; coordination even transitorily, induced non-reversible modifications. These modifications dramatically and durably accelerate peptide aggregation even in absence of Zn." Document : Thèse de Doctorat Etablissement_delivrance : Université de Toulouse 3 Date_soutenance : 17/12/2012 Ecole_doctorale : Sciences de la matière (SdM) Domaine : Chimie, biologie, santé En ligne : http://thesesups.ups-tlse.fr/1794/ Interactions of metal ions with truncated forms of amyloïd-beta linked to Alzheimer's disease [texte imprimé] / Aliès, Bruno, Auteur ; Faller, Peter, Directeur de thèse ; Hureau, Christelle, Directeur de thèse . - 2012. Langues : Anglais (eng) Tags : AMYLOID-BETA  AGGREGATION  COORDINATION  METAL IONS  CU  ZN  SPECTROSCOPIES  FLUORESCENCE Résumé : "Amyloid plaques are a hallmark of Alzheimer's disease. These plaques are formed by aggregates of amyloid beta peptides and metal ions. In this context, we studied the interaction of Cu and Zn with the truncated forms of Aß peptides. We focused on two aspect : Coordination and Aggregation. In this first part, we studied coordination of Cu on modified amyloid beta peptide compared to original peptide. These modified peptides are found in human and are considered as more deleterious. Thanks to many spectroscopies (EPR, CD, NMR...), we have shown that (i) pH depending coordination mode of amyloid beta-Cu (ii) the great matter of N-terminal in Cu coordination (iii) the major role of second sphere in coordination (iv) Cu Coordination differences between Aß and his modified forms. In the second part, our aim was to get insights into aggregation mechanisms of peptide modulate by metal ions. Aggregation of peptides is a wide field of interest from neurological diseases to nanotechnology. Thanks to different peptides (from amyloid beta) and several complementary techniques (Fluorescence, Turbitity, TEM...), we have shown that (i) the metal ions coordination dependence of aggregation (ii) acceleration of amyloid beta11-28 aggregation induced by Zn is due to a dimer formation (iii) Changes in Zn coordination induced by pH contribute to slowdown the aggregation (iv) total charge of the dimer determine the precipitation (v) Zn coordination to amyloid beta11-28 is highly dynamic ; coordination even transitorily, induced non-reversible modifications. These modifications dramatically and durably accelerate peptide aggregation even in absence of Zn." Document : Thèse de Doctorat Etablissement_delivrance : Université de Toulouse 3 Date_soutenance : 17/12/2012 Ecole_doctorale : Sciences de la matière (SdM) Domaine : Chimie, biologie, santé En ligne : http://thesesups.ups-tlse.fr/1794/

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