11 Citations (Scopus)


© 2018, © 2018 Informa UK Limited, trading as Taylor & Francis Group. Protein misfolding and aggregation into highly ordered fibrillar structures have been traditionally associated with pathological processes. Nevertheless, nature has taken advantage of the particular properties of amyloids for functional purposes, like in the protection of organisms against environmental changing conditions. Over the last decades, these fibrillar structures have inspired the design of new nanomaterials with intriguing applications in biomedicine and nanotechnology such as tissue engineering, drug delivery, adhesive materials, biodegradable nanocomposites, nanowires or biosensors. Prion and prion-like proteins, which are considered a subclass of amyloids, are becoming ideal candidates for the design of new and tunable nanomaterials. In this review, we discuss the particular properties of this kind of proteins, and the current advances on the design of new materials based on prion sequences.
Original languageEnglish
Pages (from-to)266-272
Issue number5-6
Publication statusPublished - 2 Nov 2018


  • amyloids
  • nanotechnology
  • prion forming domains
  • prion-like proteins
  • Prions
  • self-assembly


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