AMYCO: Evaluation of mutational impact on prion-like proteins aggregation propensity

Valentin Iglesias, Oscar Conchillo-Sole, Cristina Batlle, Salvador Ventura

Research output: Contribution to journalArticleResearch

14 Citations (Scopus)


© 2019 The Author(s). Background: Around 1% of human proteins are predicted to contain a disordered and low complexity prion-like domain (PrLD). Mutations in PrLDs have been shown promote a transition towards an aggregation-prone state in several diseases. Results: Recently, we have shown that an algorithm that considers the effects of mutations on PrLDs composition, as well as on localized amyloid propensity can predict the impact of these amino acid changes on protein intracellular aggregation. In this application note, we implement this concept into the AMYCO web server, a refined algorithm that forecasts the influence of amino acid changes in prion-like proteins aggregation propensity better than state-of-the-art predictors. Conclusions: The AMYCO web server allows for a fast and automated evaluation of the effect of mutations on the aggregation properties of prion-like proteins. This might uncover novel disease-linked amino acid changes in the sequences of human prion-like proteins. Additionally, it can find application in the in silico design of synthetic prion-like proteins with tuned aggregation propensities for different purposes. AMYCO does not require previous registration and is freely available to all users at:
Original languageEnglish
Article number24
JournalBMC Bioinformatics
Publication statusPublished - 14 Jan 2019


  • Amyloid
  • Prion-like domain
  • Protein aggregation
  • Protein mutation


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