Deciphering the Structure and Formation ...
Type de document :
Compte-rendu et recension critique d'ouvrage
PMID :
Titre :
Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools
Auteur(s) :
Landrieu, Isabelle [Auteur]
Biologie Structurale Intégrative [ERL 9002 - BSI ]
Facteurs de Risque et Déterminants Moléculaires des Maladies liées au Vieillissement - U 1167 [RID-AGE]
Centre Hospitalier Régional Universitaire [CHU Lille] [CHRU Lille]
Dupré, Elian [Auteur]
Biologie Structurale Intégrative [ERL 9002 - BSI ]
Facteurs de Risque et Déterminants Moléculaires des Maladies liées au Vieillissement - U 1167 [RID-AGE]
Centre Hospitalier Régional Universitaire [CHU Lille] [CHRU Lille]
Sinnaeve, Davy [Auteur]
Biologie Structurale Intégrative [ERL 9002 - BSI ]
Facteurs de Risque et Déterminants Moléculaires des Maladies liées au Vieillissement - U 1167 [RID-AGE]
Centre Hospitalier Régional Universitaire [CHU Lille] [CHRU Lille]
El Hajjar, Léa [Auteur]
Biologie Structurale Intégrative [ERL 9002 - BSI ]
Facteurs de Risque et Déterminants Moléculaires des Maladies liées au Vieillissement - U 1167 [RID-AGE]
Centre Hospitalier Régional Universitaire [CHU Lille] [CHRU Lille]
Nocca Smet, Caroline [Auteur]
Biologie Structurale Intégrative [ERL 9002 - BSI ]
Facteurs de Risque et Déterminants Moléculaires des Maladies liées au Vieillissement - U 1167 [RID-AGE]
Centre Hospitalier Régional Universitaire [CHU Lille] [CHRU Lille]
![refId](/themes/Mirage2//images/idref.png)
Biologie Structurale Intégrative [ERL 9002 - BSI ]
Facteurs de Risque et Déterminants Moléculaires des Maladies liées au Vieillissement - U 1167 [RID-AGE]
Centre Hospitalier Régional Universitaire [CHU Lille] [CHRU Lille]
Dupré, Elian [Auteur]
Biologie Structurale Intégrative [ERL 9002 - BSI ]
Facteurs de Risque et Déterminants Moléculaires des Maladies liées au Vieillissement - U 1167 [RID-AGE]
Centre Hospitalier Régional Universitaire [CHU Lille] [CHRU Lille]
Sinnaeve, Davy [Auteur]
![refId](/themes/Mirage2//images/idref.png)
Biologie Structurale Intégrative [ERL 9002 - BSI ]
Facteurs de Risque et Déterminants Moléculaires des Maladies liées au Vieillissement - U 1167 [RID-AGE]
Centre Hospitalier Régional Universitaire [CHU Lille] [CHRU Lille]
El Hajjar, Léa [Auteur]
Biologie Structurale Intégrative [ERL 9002 - BSI ]
Facteurs de Risque et Déterminants Moléculaires des Maladies liées au Vieillissement - U 1167 [RID-AGE]
Centre Hospitalier Régional Universitaire [CHU Lille] [CHRU Lille]
Nocca Smet, Caroline [Auteur]
![refId](/themes/Mirage2//images/idref.png)
Biologie Structurale Intégrative [ERL 9002 - BSI ]
Facteurs de Risque et Déterminants Moléculaires des Maladies liées au Vieillissement - U 1167 [RID-AGE]
Centre Hospitalier Régional Universitaire [CHU Lille] [CHRU Lille]
Titre de la revue :
Frontiers in Chemistry
Pagination :
886382
Éditeur :
Frontiers Media
Date de publication :
2022-05-12
Mot(s)-clé(s) en anglais :
amyloid fibril
aggregation
neurodegenerative diseases
protein semisynthesis
posttranslational modifications
native chemical ligation
fluorescent probes
nanobody
aggregation
neurodegenerative diseases
protein semisynthesis
posttranslational modifications
native chemical ligation
fluorescent probes
nanobody
Discipline(s) HAL :
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biochimie [q-bio.BM]
Résumé en anglais : [en]
Protein aggregation into highly ordered, regularly repeated cross-β sheet structures called amyloid fibrils is closely associated to human disorders such as neurodegenerative diseases including Alzheimer’s and Parkinson’s ...
Lire la suite >Protein aggregation into highly ordered, regularly repeated cross-β sheet structures called amyloid fibrils is closely associated to human disorders such as neurodegenerative diseases including Alzheimer’s and Parkinson’s diseases, or systemic diseases like type II diabetes. Yet, in some cases, such as the HET-s prion, amyloids have biological functions. High-resolution structures of amyloids fibrils from cryo-electron microscopy have very recently highlighted their ultrastructural organization and polymorphisms. However, the molecular mechanisms and the role of co-factors (posttranslational modifications, non-proteinaceous components and other proteins) acting on the fibril formation are still poorly understood. Whether amyloid fibrils play a toxic or protective role in the pathogenesis of neurodegenerative diseases remains to be elucidated. Furthermore, such aberrant protein-protein interactions challenge the search of small-molecule drugs or immunotherapy approaches targeting amyloid formation. In this review, we describe how chemical biology tools contribute to new insights on the mode of action of amyloidogenic proteins and peptides, defining their structural signature and aggregation pathways by capturing their molecular details and conformational heterogeneity. Challenging the imagination of scientists, this constantly expanding field provides crucial tools to unravel mechanistic detail of amyloid formation such as semisynthetic proteins and small-molecule sensors of conformational changes and/or aggregation. Protein engineering methods and bioorthogonal chemistry for the introduction of protein chemical modifications are additional fruitful strategies to tackle the challenge of understanding amyloid formation.Lire moins >
Lire la suite >Protein aggregation into highly ordered, regularly repeated cross-β sheet structures called amyloid fibrils is closely associated to human disorders such as neurodegenerative diseases including Alzheimer’s and Parkinson’s diseases, or systemic diseases like type II diabetes. Yet, in some cases, such as the HET-s prion, amyloids have biological functions. High-resolution structures of amyloids fibrils from cryo-electron microscopy have very recently highlighted their ultrastructural organization and polymorphisms. However, the molecular mechanisms and the role of co-factors (posttranslational modifications, non-proteinaceous components and other proteins) acting on the fibril formation are still poorly understood. Whether amyloid fibrils play a toxic or protective role in the pathogenesis of neurodegenerative diseases remains to be elucidated. Furthermore, such aberrant protein-protein interactions challenge the search of small-molecule drugs or immunotherapy approaches targeting amyloid formation. In this review, we describe how chemical biology tools contribute to new insights on the mode of action of amyloidogenic proteins and peptides, defining their structural signature and aggregation pathways by capturing their molecular details and conformational heterogeneity. Challenging the imagination of scientists, this constantly expanding field provides crucial tools to unravel mechanistic detail of amyloid formation such as semisynthetic proteins and small-molecule sensors of conformational changes and/or aggregation. Protein engineering methods and bioorthogonal chemistry for the introduction of protein chemical modifications are additional fruitful strategies to tackle the challenge of understanding amyloid formation.Lire moins >
Langue :
Anglais
Vulgarisation :
Non
Projet ANR :
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