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

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

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

4 Scopus citations

Abstract

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.

Original languageEnglish
Title of host publicationProteins in Solution and at Interfaces
Subtitle of host publicationMethods and Applications in Biotechnology and Materials Science
PublisherJohn Wiley and Sons
Pages233-282
Number of pages50
ISBN (Print)9780470952511
DOIs
StatePublished - 5 Mar 2013
Externally publishedYes

Keywords

  • Amyloid fibril formation
  • Amyloid structure
  • Nanostructured materials
  • Protein fibrillation
  • Self-assembly
  • Toxicity

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