Efficient backbone cyclization of linear peptides by a recombinant asparaginyl endopeptidase

  title={Efficient backbone cyclization of linear peptides by a recombinant asparaginyl endopeptidase},
  author={Karen S. Harris and Thomas Durek and Quentin Kaas and Aaron G. Poth and E K Gilding and Brendon Francis Conlan and Ivana Saska and Norelle L Daly and Nicole L. van der Weerden and David J. Craik and Marilyn A Anderson},
  booktitle={Nature communications},
Cyclotides are diverse plant backbone cyclized peptides that have attracted interest as pharmaceutical scaffolds, but fundamentals of their biosynthetic origin remain elusive. Backbone cyclization is a key enzyme-mediated step of cyclotide biosynthesis and confers a measure of stability on the resultant cyclotide. Furthermore, cyclization would be desirable for engineered peptides. Here we report the identification of four asparaginyl endopeptidases (AEPs), proteases implicated in cyclization… CONTINUE READING
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influences on stability and bioactivity

  • Chan, L. Y. et al. Cyclization of the antimicrobial peptide ligation
  • Chembiochem 14, 617–624
  • 2013

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