Formation of Cross-Beta Supersecondary Structure by Soft-Amyloid Cores: Strategies for Their Prediction and Characterization

M. Rosario Fernández, Irantzu Pallarès, Valentín Iglesias, Jaime Santos, Salvador Ventura

Research output: Chapter in BookChapterResearchpeer-review

1 Citation (Scopus)


© 2019, Springer Science+Business Media, LLC, part of Springer Nature. Proteins with prion-like behavior are attracting an increasing interest, since accumulating evidences indicate that they play relevant roles both in health and disease. The self-assembly of these proteins into insoluble aggregates is associated with severe neuropathological processes such as amyotrophic lateral sclerosis (ALS). However, in normal conditions, they are known to accomplish a wide range of functional roles. The conformational duality of prion-like proteins is often encoded in specific protein regions, named prion-like domains (PrLDs). PrLDs are usually long and disordered regions of low complexity. We have shown that PrLDs might contain soft-amyloid cores that contribute significantly to trigger their aggregation, as well as to support their propagation. Further exploration of the role of these sequences in the conformational conversion of prion-like proteins might provide novel insights into the mechanism of action and regulation of these polypeptides, enabling the future development of therapeutic strategies. Here, we describe a set of methodologies aimed to identify and characterize these short amyloid stretches in a protein or proteome of interest, ranging from in silico detection to in vitro and in vivo evaluation and validation.
Original languageEnglish
Title of host publicationMethods in Molecular Biology
Number of pages25
ISBN (Electronic)1940-6029
Publication statusPublished - 1 Jan 2019

Publication series

NameMethods in Molecular Biology


  • Amyloid
  • Bioinformatics
  • Cross-beta-sheet
  • Fibril
  • Prion-like
  • Protein aggregation
  • Soft-amyloid core


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