The renaissance of peptides as prospective therapeutics has fostered the development of novel strategies for their synthesis and modification. In this context, besides the developmentofnewchemicalpeptideligationapproaches,especiallytheuseofenzymes as a versatile tool has gained increased attention. Nowadays, due to their inherent properties such as excellent regio- and chemoselectivity, enzymes represent invaluable instruments in both academic and industrial laboratories. This mini-review focuses on natural- and engineered peptide ligases that can form a new peptide (amide) bond between the C-terminal carboxy and N-terminal amino group of a peptide and/or protein. The pro’s and cons of several enzyme classes such as Sortases, Asparaginyl Endoproteases, Trypsin relatedenzymesand as a centralfocus subtilisin-derived variants are summarized. Most recent developments with regards to ligation and cyclization are highlighted

Natural Occurring and Engineered Enzymes for Peptide Ligation and Cyclization

Cabri W
2019

Abstract

The renaissance of peptides as prospective therapeutics has fostered the development of novel strategies for their synthesis and modification. In this context, besides the developmentofnewchemicalpeptideligationapproaches,especiallytheuseofenzymes as a versatile tool has gained increased attention. Nowadays, due to their inherent properties such as excellent regio- and chemoselectivity, enzymes represent invaluable instruments in both academic and industrial laboratories. This mini-review focuses on natural- and engineered peptide ligases that can form a new peptide (amide) bond between the C-terminal carboxy and N-terminal amino group of a peptide and/or protein. The pro’s and cons of several enzyme classes such as Sortases, Asparaginyl Endoproteases, Trypsin relatedenzymesand as a centralfocus subtilisin-derived variants are summarized. Most recent developments with regards to ligation and cyclization are highlighted
2019
Timo Nuijens; Ana Toplak; Marcel Schmidt; Antonio Ricci; Cabri W
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/756714
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