Mining and engineering activity in catalytic amyloids

Samuel Peña-Díaz, Pedro Ferreira, Maria João Ramos, Daniel E Otzen*

*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review


This chapter describes how to test different amyloid preparations for catalytic properties. We describe how to express, purify, prepare and test two types of pathological amyloid (tau and α-synuclein) and two functional amyloid proteins, namely CsgA from Escherichia coli and FapC from Pseudomonas. We therefore preface the methods section with an introduction to these two examples of functional amyloid and their remarkable structural and kinetic properties and high physical stability, which renders them very attractive for a range of nanotechnological designs, both for structural, medical and catalytic purposes. The simplicity and high surface exposure of the CsgA amyloid is particularly useful for the introduction of new functional properties and we therefore provide a computational protocol to graft active sites from an enzyme of interest into the amyloid structure. We hope that the methods described will inspire other researchers to explore the remarkable opportunities provided by bacterial functional amyloid in biotechnology.

Original languageEnglish
Book seriesMethods in Enzymology
Pages (from-to)345-422
Number of pages78
Publication statusPublished - 2024


  • Amyloid/chemistry
  • Bacterial Proteins/chemistry
  • Catalysis
  • Catalytic Domain
  • Escherichia coli Proteins/metabolism
  • Escherichia coli/genetics
  • Humans
  • Protein Engineering/methods
  • Pseudomonas/metabolism
  • alpha-Synuclein/chemistry
  • tau Proteins/metabolism
  • Catalytic assays
  • QM/MM
  • Amyloid formation
  • Computational analysis
  • Functional and pathological amyloid
  • Chromogenic substrates


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