Biomimetic synthesis and optimization of cyclic peptide antibiotics

@article{Kohli2002BiomimeticSA,
  title={Biomimetic synthesis and optimization of cyclic peptide antibiotics},
  author={Rahul M. Kohli and Christopher T Walsh and Michael D. Burkart},
  journal={Nature},
  year={2002},
  volume={418},
  pages={658-661}
}
Molecules in nature are often brought to a bioactive conformation by ring formation (macrocyclization). A recurrent theme in the enzymatic synthesis of macrocyclic compounds by non-ribosomal and polyketide synthetases is the tethering of activated linear intermediates through thioester linkages to carrier proteins, in a natural analogy to solid-phase synthesis. A terminal thioesterase domain of the synthetase catalyses release from the tether and cyclization. Here we show that an isolated… 

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Cyclization of Fungal Nonribosomal Peptides by a Terminal Condensation-Like Domain

Evidence of a likely universal macrocyclization strategy employed by fungal NRPSs is provided and extensive biochemical and mutational studies confirmed the essential role of the CT domain in catalyzing cyclization in a thiolation domain-dependent fashion.

Synthesis of peptides and pyrazines from β-amino alcohols through extrusion of H2 catalyzed by ruthenium pincer complexes: ligand-controlled selectivity.

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Biosynthetic Strategies for Macrocyclic Peptides

This review highlights the broad spectrum of strategy classes, novel platforms, structure diversity, chemical space, and functionalities of macrocyclic peptides enabled by emerging biosynthetic platforms to achieve bioactivity and for therapeutic purposes.
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