Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association

Jaime Santos Suarez*, Irantzu Pallares Goitiz, Juan Valentin Iglesias Mas, Salvador Ventura Zamora*

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

9 Citations (Scopus)


The amyloid conformation is considered a fundamental state of proteins and the propensity to populate it a generic property of polypeptides. Multiple proteome-wide analyses addressed the presence of amyloidogenic regions in proteins, nurturing our understanding of their nature and biological implications. However, these analyses focused on highly aggregation-prone and hydrophobic stretches that are only marginally found in intrinsically disordered regions (IDRs). Here, we explore the prevalence of cryptic amyloidogenic regions (CARs) of polar nature in IDRs. CARs are widespread in IDRs and associated with IDPs function, with particular involvement in protein–protein interactions, but their presence is also connected to a risk of malfunction. By exploring this function/malfunction dichotomy, we speculate that ancestral CARs might have evolved into functional interacting regions playing a significant role in protein evolution at the origins of life.

Original languageEnglish
Pages (from-to)4192–4206
Number of pages15
JournalComputational and Structural Biotechnology Journal
Publication statusPublished - 23 Jul 2021


  • Aggregation
  • Amyloid
  • Evolution
  • Intrinsically disordered proteins
  • Protein disorder
  • Protein–protein interactions


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