Amyloid-Like Fibrils: Origin, Structure, Properties, and Potential Technological Applications

Pablo Taboada*, Silvia Barbosa, Josué Juárez, Manuel Alatorre Meda, Víctor Mosquera

*Autor correspondiente de este trabajo

Producción científica: Capítulo del libro/informe/acta de congresoCapítulorevisión exhaustiva

4 Citas (Scopus)

Resumen

This chapter provides an overview about the origin of amyloid fibril formation, and the main characteristics of their self-assembly process and structure. First, the chapter comments on the mechanisms by which proteins can self-assemble and how they can reach a hierarchically well-ordered assembled state more stable than the native one. It presents different models which explain several complex steps taking part in fibrillogenesis. Next, it explains the most common features and characteristics of both the amyloid formation process and the amyloid structure, respectively. Then, the chapter establishes the origins of amyloid toxicity and the different alternatives provided by nature or developed by researchers to reduce/inhibit their adverse effects. Finally, it shows how nature finds important functionalities to the amyloid fold thanks to their special structural and physicochemical properties. The chapter also shows how humans can exploit the superior advantages of these nanostructured materials compared to others for new emerging applications.

Idioma originalInglés
Título de la publicación alojadaProteins in Solution and at Interfaces
Subtítulo de la publicación alojadaMethods and Applications in Biotechnology and Materials Science
EditorialJohn Wiley and Sons
Páginas233-282
Número de páginas50
ISBN (versión impresa)9780470952511
DOI
EstadoPublicada - 5 mar. 2013
Publicado de forma externa

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