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- W2137990147 endingPage "1240" @default.
- W2137990147 startingPage "1232" @default.
- W2137990147 abstract "Abstract 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." @default.
- W2137990147 created "2016-06-24" @default.
- W2137990147 creator A5073891795 @default.
- W2137990147 creator A5083922106 @default.
- W2137990147 date "2010-12-29" @default.
- W2137990147 modified "2023-10-18" @default.
- W2137990147 title "9-Fluorenylmethoxycarbonyl-Based Solid-Phase Synthesis of Peptide α-Thioesters" @default.
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