Jump to main content
Jump to site search

Issue 36, 2011
Previous Article Next Article

Ribosomal synthesis of backbone macrocyclic peptides

Author affiliations

Abstract

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

Back to tab navigation

Publication details

The article was received on 05 May 2011, accepted on 24 Jun 2011 and first published on 15 Jul 2011


Article type: Highlight
DOI: 10.1039/C1CC12647D
Citation: Chem. Commun., 2011,47, 9946-9958
  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements