NDLI: Accelerating chemoselective peptide bond formation using bis(2-selenylethyl)amido peptide selenoester surrogates

Content Provider	Royal Society of Chemistry (RSC)
Author	Cargoët, Marine Boll, Emmanuelle Chang, Yun Min Desmet, Rémi Ollivier, Nathalie Raibaut, Laurent Drobecq, Hervé Melnyk, Oleg Monbaliu, Jean-Christophe M.
Copyright Year	2016
Abstract	Given the potential of peptide selenoesters for protein total synthesis and the paucity of methods for the synthesis of these sensitive peptide derivatives, we sought to explore the usefulness of the bis(2-selenylethyl)amido (SeEA) group, i.e. the selenium analog of the bis(2-sulfanylethyl)amido (SEA) group, for accelerating peptide bond formation. A chemoselective exchange process operating in water was devised for converting SEA peptides into the SeEA ones. Kinetic studies show that SeEA ligation, which relies on an initial N,Se-acyl shift process, proceeds significantly faster than SEA ligation. This property enabled the design of a kinetically controlled three peptide segment assembly process based on the sequential use of SeEA and SEA ligation reactions. The method was validated by the total synthesis of hepatocyte growth factor K1 (85 AA) and biotinylated NK1 (180 AA) domains.
Starting Page	2657
Ending Page	2665
Page Count	9
File Format	HTM / HTML PDF
ISSN	20416520
Volume Number	7
Issue Number	4
Journal	Chemical Science
DOI	10.1039/c5sc03459k
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Peptide bond Selenium Tachykinin receptor 1 Peptide SEA Protein Total synthesis Chemical ligation Growth factor
Content Type	Text
Resource Type	Article
Subject	Chemistry

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