2013年9月21日
Stereoselective synthesis of Arabidopsis CLAVATA3 (CLV3) glycopeptide, unique protein post-translational modifications of secreted peptide hormone in plant
Organic and Biomolecular Chemistry
- ,
- ,
- 巻
- 11
- 号
- 35
- 開始ページ
- 5892
- 終了ページ
- 5907
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1039/c3ob41212a
The unique hydroxylproline (Hyp)-linked O-glycan modification is a common process in hydroxyproline-rich glycoproteins (HRGPs). The modification occurs through post-translational hydroxylation at 4-position of proline residues some of which are followed by O-glycosylation at the resulting Hyp which is also found in some secreted peptide hormones such as CLAVATA3 (CLV3) of Arabidopsis thaliana plants. An active mature CLV3 is a tridecapeptide linked to β-l-Araf-(1→2)-β-l-Araf-(1→2)-β-l-Araf at a Hyp residue in the center of the peptide sequence such as Arg-Thr-Val-Hyp-Ser-Gly-Hyp(l- Arafn)-Asp-Pro-Leu-His-His-His (n = 3). We report here the synthesis of the secreted and modified CLV3 glycopeptide with all glycoforms (Araf 0-3CLV3) of A. thaliana plants. A highly stereoselective β-arabinofuranosylation of Hyp derivatives as the key step of the synthesis of CLV3 glycopeptide was achieved by NAP ether-mediated IAD, which was effectively applied to the synthesis of oligoarabinosylated hydroxylproline [Hyp(l-Araf1-3)] derivatives. Fmoc-solid phase peptide synthesis was carried out using COMU as the coupling reagent for the introduction of [Hyp(l-Araf0-3)] derivatives as well as further elongation to the CLV3 glycopeptides. © 2013 The Royal Society of Chemistry.
- リンク情報
- ID情報
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- DOI : 10.1039/c3ob41212a
- ISSN : 1477-0520
- ORCIDのPut Code : 33943273
- PubMed ID : 23912193
- SCOPUS ID : 84882358471
- Web of Science ID : WOS:000323866400015