Sortase A-mediated on-resin peptide cleavage and in situ ligation: an efficient one-pot strategy for the synthesis of functional peptides and proteins

文献情報

出版日 2017-07-17

DOI 10.1039/C7QO00481H

インパクトファクター 5.281

著者

Xiaozhong Cheng, Tao Zhu, Haofei Hong, Zhifang Zhou, Zhimeng Wu

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要旨

Sortase A was firstly found to recognize a PEGA resin supported peptide donor containing a LPXTG motif and to ligate with a suitable acceptor containing oligo-glycine to afford conjugates in one-pot. This approach combining enzymatic on-resin cleavage, activation and in situ ligation, was employed to synthesize dual functional peptides, modify peptides with lipids, biotin and PEG, as well as protein N-terminal labeling in high efficiency.

掲載誌

Organic Chemistry Frontiers

CiteScore: 7.8

自己引用率: 8.7%

年間論文数: 724

Organic Chemistry Frontiers publishes high-quality research from across organic chemistry. Emphases are placed on studies that make significant contributions to the field of organic chemistry by reporting either new or significantly improved protocols or methodologies. Topics include, but are not limited to the following: Organic synthesis Development of synthetic methodologies Catalysis Natural products Functional organic materials Supramolecular and macromolecular chemistry Physical and computational organic chemistry

Sortase A-mediated on-resin peptide cleavage and in situ ligation: an efficient one-pot strategy for the synthesis of functional peptides and proteins

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