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Showing 1–4 of 4 results
Advanced filters: Author: David L. Niquille Clear advanced filters
  • Nonribosomal peptide synthetases (NRPSs) produce vital natural products but have proven recalcitrant to biosynthetic engineering. Now, a combination of yeast surface display and fluorescence-activated cell sorting (FACS) has been used to reprogram an L-Phe-incorporating module for β-Phe. The resulting module is highly selective and functions efficiently in NRPS pathways.

    • David L. Niquille
    • Douglas A. Hansen
    • Donald Hilvert
    Research
    Nature Chemistry
    Volume: 10, P: 282-287
  • Nonribosomal peptide synthetases produce valuable natural products but are challenging to engineer. Yeast surface display and fluorescence-activated cell sorting have now been combined to reprogram a condensation domain to recognize a noncanonical lipid substrate. This methodology may facilitate molecular tailoring of many biosynthetic assembly lines.

    • Ines B. Folger
    • Natália F. Frota
    • Donald Hilvert
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 20, P: 761-769
  • Combining enzymes from different pathways in nature could enable de novo peptide design, but determining enzyme-specificity rules is non-trivial. Here a biophysical model combining enzymes sourced from bacterial ribosomally synthesized and post-translationally modified peptide (RiPP) gene clusters was generated to formalize enzyme-specificity rules and create peptide scaffolds with defined post-translational modifications.

    • Emerson Glassey
    • Zhengan Zhang
    • Christopher A. Voigt
    Research
    Nature Chemistry
    Volume: 17, P: 233-245
  • Peptide secondary metabolites have a diverse range of functions. Here the authors present a method to design and screen a large library of modified peptides in E. coli against a target of interest.

    • Andrew M. King
    • Daniel A. Anderson
    • Christopher A. Voigt
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12