Butelase-mediated synthesis of protein thioesters and its application for tandem chemoenzymatic ligation

Using a recently discovered peptide ligase, butelase 1, we developed a novel method to access protein thioesters in good yield. We successfully combined it with native chemical ligation and sortase-mediated ligation in tandem for protein C-terminal labeling and dual-terminal labeling to exploit the...

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Main Authors: Cao, Yuan, Nguyen, Kien Truc Giang, Tam, James P., Liu, Chuan-Fa
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2016
Subjects:
Online Access:https://hdl.handle.net/10356/81837
http://hdl.handle.net/10220/39726
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-818372023-02-28T16:58:26Z Butelase-mediated synthesis of protein thioesters and its application for tandem chemoenzymatic ligation Cao, Yuan Nguyen, Kien Truc Giang Tam, James P. Liu, Chuan-Fa School of Biological Sciences catalytic efficiency thioester Using a recently discovered peptide ligase, butelase 1, we developed a novel method to access protein thioesters in good yield. We successfully combined it with native chemical ligation and sortase-mediated ligation in tandem for protein C-terminal labeling and dual-terminal labeling to exploit the orthogonality of these three ligation methods. NRF (Natl Research Foundation, S’pore) Accepted version 2016-01-21T03:08:59Z 2019-12-06T14:41:14Z 2016-01-21T03:08:59Z 2019-12-06T14:41:14Z 2015 Journal Article Cao, Y., Nguyen, G. K. T., Tam, J. P., & Liu, C.-F. (2015). Butelase-mediated synthesis of protein thioesters and its application for tandem chemoenzymatic ligation. Chem. Commun., 51(97), 17289-17292. 1359-7345 https://hdl.handle.net/10356/81837 http://hdl.handle.net/10220/39726 10.1039/C5CC07227A en Chemical Communications © 2015 The Royal Society of Chemistry. This is the author created version of a work that has been peer reviewed and accepted for publication by Chemical Communications, The Royal Society of Chemistry. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1039/C5CC07227A]. 4 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic catalytic efficiency
thioester
spellingShingle catalytic efficiency
thioester
Cao, Yuan
Nguyen, Kien Truc Giang
Tam, James P.
Liu, Chuan-Fa
Butelase-mediated synthesis of protein thioesters and its application for tandem chemoenzymatic ligation
description Using a recently discovered peptide ligase, butelase 1, we developed a novel method to access protein thioesters in good yield. We successfully combined it with native chemical ligation and sortase-mediated ligation in tandem for protein C-terminal labeling and dual-terminal labeling to exploit the orthogonality of these three ligation methods.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Cao, Yuan
Nguyen, Kien Truc Giang
Tam, James P.
Liu, Chuan-Fa
format Article
author Cao, Yuan
Nguyen, Kien Truc Giang
Tam, James P.
Liu, Chuan-Fa
author_sort Cao, Yuan
title Butelase-mediated synthesis of protein thioesters and its application for tandem chemoenzymatic ligation
title_short Butelase-mediated synthesis of protein thioesters and its application for tandem chemoenzymatic ligation
title_full Butelase-mediated synthesis of protein thioesters and its application for tandem chemoenzymatic ligation
title_fullStr Butelase-mediated synthesis of protein thioesters and its application for tandem chemoenzymatic ligation
title_full_unstemmed Butelase-mediated synthesis of protein thioesters and its application for tandem chemoenzymatic ligation
title_sort butelase-mediated synthesis of protein thioesters and its application for tandem chemoenzymatic ligation
publishDate 2016
url https://hdl.handle.net/10356/81837
http://hdl.handle.net/10220/39726
_version_ 1759854915148054528