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ID 111890
著者
Naruse, Naoto Tokushima University
Ohkawachi, Kento Tokushima University
資料タイプ
学術雑誌論文
抄録
Resin-bound N–sulfanylethylanilide (SEAlide) peptide was found to function as a crypto-thioester peptide. Exposure of the peptide resin to an aqueous solution under neutral conditions in the presence of thiols affords thioesters without accompanying racemization of C-terminal amino acids. Furthermore, the resin-bound SEAlide peptides react with N-terminal cysteinyl peptides in the absence of phosphate salts to afford ligated products, whereas soluble SEAlide peptides do not. This unexpected difference in reactivity of the SEAlide peptides allows for a one-pot/three-fragment ligation using resin-bound and unbound peptides.
掲載誌名
Organic Letters
ISSN
15237060
15237052
cat書誌ID
AA11347843
AA1218968X
出版者
ACS publications
20
8
開始ページ
2449
終了ページ
2453
発行日
2018-04-09
権利情報
This document is the Accepted Manuscript version of a Published Work that appeared in final form in Organic Letters, copyright ©American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.orglett.8b00795.
EDB ID
出版社版DOI
出版社版URL
フルテキストファイル
言語
eng
著者版フラグ
著者版
部局
薬学系