Butelase 1: A Versatile Ligase for Peptide and Protein Macrocyclization
Macrocyclization is a valuable tool for drug design and protein engineering. Although various methods have been developed to prepare macrocycles, a general and efficient strategy is needed. Here we report a highly efficient method using butelase 1 to macrocyclize peptides and proteins ranging in siz...
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sg-ntu-dr.10356-817132023-02-28T16:58:41Z Butelase 1: A Versatile Ligase for Peptide and Protein Macrocyclization Nguyen, Giang Kien Truc Kam, Antony Tam, James Pingkwan Loo, Shining Jansson, Anna Elisabet Pan, Lucy Xin School of Biological Sciences Biological Sciences Macrocyclization is a valuable tool for drug design and protein engineering. Although various methods have been developed to prepare macrocycles, a general and efficient strategy is needed. Here we report a highly efficient method using butelase 1 to macrocyclize peptides and proteins ranging in sizes from 26 to >200 residues. We achieved cyclizations that are 20,000 times faster than sortase A, the most widely used ligase for protein cyclization. The reactions completed within minutes with up to 95% yields. NRF (Natl Research Foundation, S’pore) Published version 2016-01-11T05:27:39Z 2019-12-06T14:36:42Z 2016-01-11T05:27:39Z 2019-12-06T14:36:42Z 2015 Journal Article Nguyen, G. K. T., Kam, A., Loo, S., Jansson, A. E., Pan, L. X., & Tam, J. P. (2015). Butelase 1: A Versatile Ligase for Peptide and Protein Macrocyclization. Journal of the American Chemical Society, 137(49), 15398-15401. 0002-7863 https://hdl.handle.net/10356/81713 http://hdl.handle.net/10220/39652 10.1021/jacs.5b11014 en Journal of the American Chemical Society © 2015 American Chemical Society. This paper was published in Journal of the American Chemical Society and is made available as an electronic reprint (preprint) with permission of American Chemical Society. The published version is available at: [http://dx.doi.org/10.1021/jacs.5b11014]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law. 4 p. application/pdf |
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Biological Sciences Nguyen, Giang Kien Truc Kam, Antony Tam, James Pingkwan Loo, Shining Jansson, Anna Elisabet Pan, Lucy Xin Butelase 1: A Versatile Ligase for Peptide and Protein Macrocyclization |
| description |
Macrocyclization is a valuable tool for drug design and protein engineering. Although various methods have been developed to prepare macrocycles, a general and efficient strategy is needed. Here we report a highly efficient method using butelase 1 to macrocyclize peptides and proteins ranging in sizes from 26 to >200 residues. We achieved cyclizations that are 20,000 times faster than sortase A, the most widely used ligase for protein cyclization. The reactions completed within minutes with up to 95% yields. |
| author2 |
School of Biological Sciences |
| author_facet |
School of Biological Sciences Nguyen, Giang Kien Truc Kam, Antony Tam, James Pingkwan Loo, Shining Jansson, Anna Elisabet Pan, Lucy Xin |
| format |
Article |
| author |
Nguyen, Giang Kien Truc Kam, Antony Tam, James Pingkwan Loo, Shining Jansson, Anna Elisabet Pan, Lucy Xin |
| author_sort |
Nguyen, Giang Kien Truc |
| title |
Butelase 1: A Versatile Ligase for Peptide and Protein Macrocyclization |
| title_short |
Butelase 1: A Versatile Ligase for Peptide and Protein Macrocyclization |
| title_full |
Butelase 1: A Versatile Ligase for Peptide and Protein Macrocyclization |
| title_fullStr |
Butelase 1: A Versatile Ligase for Peptide and Protein Macrocyclization |
| title_full_unstemmed |
Butelase 1: A Versatile Ligase for Peptide and Protein Macrocyclization |
| title_sort |
butelase 1: a versatile ligase for peptide and protein macrocyclization |
| publishDate |
2016 |
| url |
https://hdl.handle.net/10356/81713 http://hdl.handle.net/10220/39652 |
| _version_ |
1759858293529903104 |