Prion domains as a driving force for the assembly of functional nanomaterials

Weiqiang Wang, Salvador Ventura*

*Corresponding author for this work

Research output: Contribution to journalReview articleResearchpeer-review

5 Citations (Scopus)


Amyloids display a highly ordered fibrillar structure. Many of these assemblies appear associated with human disease. However, the controllable, stable, tunable, and robust nature of amyloid fibrils can be exploited to build up remarkable nanomaterials with a wide range of applications in biomedicine and biotechnology. Functional prions constitute a particular class of amyloids. These transmissible proteins exhibit a modular architecture, with a disordered prion domain responsible for the assembly and one or more globular domains that account for the activity. Importantly, the original globular protein can be replaced with any protein of interest, without compromising the fibrillation potential. These genetic fusions form fibrils in which the globular domain remains folded, rendering functional nanostructures. However, in some cases, steric hindrance restricts the activity of these fibrils. This limitation can be solved by dissecting prion domains into shorter sequences that keep their self-assembling properties while allowing better access to the active protein in the fibrillar state. In this review, we will discuss the properties of prion-like functional nanomaterials and the amazing applications of these biocompatible fibrillar arrangements.

Original languageEnglish
Pages (from-to)170-179
Number of pages10
Issue number1
Publication statusPublished - 1 Jan 2020


  • Prions
  • amyloids
  • nanomaterials
  • prion-like domains
  • self-assembly
  • yeast


Dive into the research topics of 'Prion domains as a driving force for the assembly of functional nanomaterials'. Together they form a unique fingerprint.

Cite this