Peptide 9

Peptide thioesters play a key role in convergent protein synthesis strategies such as native chemical ligation, traceless Staudinger ligation, and Ag(+) -mediated thioester ligation. The Boc-based solid-phase synthesis provides a very reliable access to peptide thioesters. However, the acid lability of many peptide modifications and the requirements of most parallel peptide synthesizers call for the milder Fmoc-based solid-phase synthesis. The Fmoc-based synthesis of peptide thioesters is more cumbersome and typically proceeds with lower yields than the synthesis of peptide acids and peptide amides. The success of native chemical ligation and related technologies has sparked intensive research effort devoted to the development of new methods. The recent progress in this rapidly expanding field is reviewed.

Covering1993 up to May 2020 Linaridins, defined as linear, dehydrated (arid) peptides, are a small but growing family of natural products belonging to the ribosomally synthesized and post-translationally modified peptide (RiPP) superfamily. To date, only a few members of the linaridin family have been characterized; however, in silico analysis has shown that this family of RiPPs is widespread in nature with high structural diversity. Unlike the case of most of the dehydroamino acid-containing RiPPs, such as lanthipeptides and thiopeptides, in which dehydroamino acids are produced by lanthipeptide dehydratase-like enzymes, in linaridins, dehydroamino acids are produced by a distinct set of enzymes with still unknown biochemistry. In this Highlight we have discussed the structural features, classification, biosynthesis, engineering, and widespread occurrence of linaridins and highlighted several intriguing issues in the maturation of this RiPP family.