| Item type |
文献 / Documents(1) |
| 公開日 |
2018-07-13 |
| アクセス権 |
|
|
アクセス権 |
open access |
| 資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
| 出版社版DOI |
|
|
|
関連識別子 |
https://doi.org/10.1002/cbic.201600400 |
|
|
関連名称 |
10.1002/cbic.201600400 |
| 出版タイプ |
|
|
出版タイプ |
AM |
|
出版タイプResource |
http://purl.org/coar/version/c_ab4af688f83e57aa |
| タイトル |
|
|
タイトル |
Tailored Synthesis of 162-Residue S-Monoglycosylated GM2-Activator Protein (GM2AP) Analogues that Allows Facile Access to Protein Library |
| 著者 |
ナカムラ, タカヒロ
サトウ, コウヘイ
ナルセ, ナオト
キタカゼ, ケイスケ
猪熊, 翼
ヒロカワ, タカツグ
重永, 章
伊藤, 孝司
大髙, 章
|
| 抄録 |
|
|
内容記述 |
A synthetic protocol has been developed for the preparation of 162-residue S-monoglycosylated GM2-activator protein (GM2AP) analogues bearing various amino acid substitutions for Thr69. The facile incorporation of the replacements into the protein was achieved by a one-pot/N–to–C-directed sequential ligation strategy using readily accessible middle N-sulfanylethylanilide (SEAlide) peptides consisting of seven amino acid residues. A kinetically-controlled ligation protocol was successfully applied to the assembly of three peptide segments covering the GM2AP. The native chemical ligation (NCL) reactivities of the SEAlide can be tuned by the presence or absence of phosphate salts. Furthermore, the NCL of the alkyl thioester fragment (GM2AP (1–31)) with the N-terminal cysteinyl prolyl thioester (GM2AP (32–67)) proceeded smoothly to yield the 67-residue prolyl thioester, with the prolyl thioester moiety remaining intact. This newly developed strategy enabled the facile synthesis of GM2AP analogues. Thus, we refered this synthetic protocol as “Tailored Synthesis” for the construction of a GM2AP library. |
| キーワード |
|
|
主題 |
native chemical ligation |
| キーワード |
|
|
主題 |
prolyl thioester |
| キーワード |
|
|
主題 |
N-sulfanylethylanilide |
| キーワード |
|
|
主題 |
kinetically-controlled ligation |
| キーワード |
|
|
主題 |
GM2AP |
| 書誌情報 |
en : ChemBioChem
巻 17,
号 20,
p. 1986-1992,
発行日 2016-08-19
|
| 収録物ID |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
14397633 |
| 収録物ID |
|
|
収録物識別子タイプ |
NCID |
|
収録物識別子 |
AA11617132 |
| 収録物ID |
|
|
収録物識別子タイプ |
NCID |
|
収録物識別子 |
AA11497584 |
| 出版者 |
|
|
出版者 |
WILEY-VCH Verlag GmbH & Co. KGaA |
| 権利情報 |
|
|
権利情報 |
This is the peer-reviewed version of the following article: T. Nakamura, K. Sato, N. Naruse, K. Kitakaze, T. Inokuma, T. Hirokawa, A. Shigenaga, K. Itoh, A. Otaka (2016), Tailored Synthesis of 162‐Residue S‐Monoglycosylated GM2‐Activator Protein (GM2AP) Analogues that Allows Facile Access to a Protein Library. ChemBioChem Vol.17 Issue20 p 1986-1992 doi:10.1002/cbic.201600400, which has been published in final form at https://doi.org/10.1002/cbic.201600400.
This article may be used for non-commercial purposes in accordance with Wiley-VCH Terms and Conditions for Self-Archiving. |
| EID |
|
|
識別子 |
314628 |
| 言語 |
|
|
言語 |
eng |
cbic_17_20_1986.pdf (1.26 MB)
