Highlighted Paper selected by Editor-in-Chief : Sequence-Independent Traceless Method for Preparation of Peptide/Protein Thioesters Using CPaseY-Mediated Hydrazinolysis
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- Ueda Masahiro
- Institute of Biomedical Sciences and Graduate School of Pharmaceutical Sciences, Tokushima University
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- Komiya Chiaki
- Institute of Biomedical Sciences and Graduate School of Pharmaceutical Sciences, Tokushima University
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- Arii Sayuki
- Institute of Biomedical Sciences and Graduate School of Pharmaceutical Sciences, Tokushima University
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- Kusumoto Kohshi
- Institute of Biomedical Sciences and Graduate School of Pharmaceutical Sciences, Tokushima University
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- Denda Masaya
- Institute of Biomedical Sciences and Graduate School of Pharmaceutical Sciences, Tokushima University
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- Okuhira Keiichiro
- Institute of Biomedical Sciences and Graduate School of Pharmaceutical Sciences, Tokushima University Osaka University of Pharmaceutical Sciences
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- Shigenaga Akira
- Institute of Biomedical Sciences and Graduate School of Pharmaceutical Sciences, Tokushima University Faculty of Pharmacy and Pharmaceutical Sciences, Fukuyama University
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- Otaka Akira
- Institute of Biomedical Sciences and Graduate School of Pharmaceutical Sciences, Tokushima University
書誌事項
- タイトル別名
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- Sequence-Independent Traceless Method for Preparation of Peptide/Protein Thioesters Using CPaseY-Mediated Hydrazinolysis
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<p>Proteins incorporating artificial moieties such as fluorophores and drugs have enjoyed increasing use in chemical biology and drug development research. Preparation of such artificial protein derivatives has relied mainly on native chemical ligation in which peptide/protein thioesters chemoselectively react with N-terminal cysteine (Cys) peptides to afford protein molecules. The protein thioesters derived from expressed proteins represent thioesters that are very useful for the preparation of artificial proteins by native chemical ligation with synthetic peptides with N-terminal Cys. We recently have developed a traceless thioester-producing protocol using carboxypeptidase Y (CPaseY) which is compatible with an expressed protein. The traceless character is ensured by CPaseY-mediated hydrazinolysis of C-terminal Xaa (X)-Cys-proline (Pro)-leucine (Leu)-OH sequence followed by an auto-processing of the Cys-Pro (CP) dipeptide unit, affording the corresponding X-thioester (X-SR). However, hydrazinolysis of the amide bond in the prolyl leucine junction depends significantly on the nature of X. In the case of hydrophobic X residues, the hydrazinolysis overreacts to give several hydrazides while the reaction of hydrophilic X residues proceeds slowly. In this research, we attempted to develop an X-independent CPaseY-mediated protocol and found that the incorporation of a triple CP sequence into the C-terminal end (X-(CP)3-Leu-OH) allows for efficient X-SR formation in a manner that is independent of X.</p>
収録刊行物
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- CHEMICAL & PHARMACEUTICAL BULLETIN
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CHEMICAL & PHARMACEUTICAL BULLETIN 68 (12), 1226-1232, 2020-12-01
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1391975276373164672
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- NII論文ID
- 130007948412
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- NII書誌ID
- AA00602100
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- ISSN
- 13475223
- 00092363
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- NDL書誌ID
- 030781777
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- PubMed
- 33028801
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
- KAKEN
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- 抄録ライセンスフラグ
- 使用不可