2011年2月
Synthesis of the sphingolipid activator protein, saposin C, using an azido-protected O-acyl isopeptide as an aggregation-disrupting element
TETRAHEDRON LETTERS
- ,
- ,
- ,
- ,
- ,
- ,
- ,
- ,
- 巻
- 52
- 号
- 5
- 開始ページ
- 635
- 終了ページ
- 639
- 記述言語
- 英語
- 掲載種別
- 研究論文（学術雑誌）
- DOI
- 10.1016/j.tetlet.2010.11.154
- 出版者・発行元
- PERGAMON-ELSEVIER SCIENCE LTD
In order to achieve an efficient synthesis of highly hydrophobic proteins by the native chemical ligation (NCL) reaction, we examined to incorporate the O-acyl isopeptide method, which is known to improve the solubility of the segment, to the NCL reaction: a peptide thioester having O-acyl isopeptide structures is prepared by the Boc mode solid-phase method using an azido group as a protecting group for the isopeptide site, and then ligated with C-terminal segment with an in situ reduction of the azido group followed by an O- to N-acyl shift. This method was successfully applied to the synthesis of the sphingolipid activator protein, saposin C. (C) 2010 Elsevier Ltd. All rights reserved.
- リンク情報
- ID情報
-
- DOI : 10.1016/j.tetlet.2010.11.154
- ISSN : 0040-4039
- Web of Science ID : WOS:000286997100021