Jump to main content
Jump to site search

Issue 10, 2017
Previous Article Next Article

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

Author affiliations

Abstract

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.

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 17 Jun 2017, accepted on 16 Jul 2017 and first published on 17 Jul 2017


Article type: Research Article
DOI: 10.1039/C7QO00481H
Citation: Org. Chem. Front., 2017,4, 2058-2062
  •   Request permissions

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

    X. Cheng, T. Zhu, H. Hong, Z. Zhou and Z. Wu, Org. Chem. Front., 2017, 4, 2058
    DOI: 10.1039/C7QO00481H

Search articles by author

Spotlight

Advertisements