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Issue 36, 2011
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Ribosomal synthesis of backbone macrocyclic peptides

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A wealth of knowledge has been accumulated on ribosomal synthesis of macrocyclic peptides in the past decade. In nature, backbone cyclization of the translated linear peptides is generally catalyzed by specific enzymes, giving them peptidase resistance, thermodynamic stability and various other physiological activities. Due to these biochemical traits, backbone cyclic peptides have become an attractive resource for the discovery of drug leads. Recently, various new methodologies have also been established to generate man-made cyclic peptides. Here, we describe the biosynthetic mechanisms of naturally occurring backbone macrocyclic peptides focusing on cyclotides, sunflower trypsin inhibitors (SFTIs) and cyanobactins as well as several new emerging methodologies, such as sortase mediated ligation, protein splicing method and genetic code reprogramming.

Graphical abstract: Ribosomal synthesis of backbone macrocyclic peptides

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Article information

05 May 2011
24 Jun 2011
First published
15 Jul 2011

Chem. Commun., 2011,47, 9946-9958
Article type

Ribosomal synthesis of backbone macrocyclic peptides

T. Katoh, Y. Goto, Md. S. Reza and H. Suga, Chem. Commun., 2011, 47, 9946
DOI: 10.1039/C1CC12647D

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