Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81713
Title: Butelase 1: A Versatile Ligase for Peptide and Protein Macrocyclization
Authors: Nguyen, Giang Kien Truc
Kam, Antony
Tam, James Pingkwan
Loo, Shining
Jansson, Anna Elisabet
Pan, Lucy Xin
Keywords: Biological Sciences
Issue Date: 2015
Source: 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.
Series/Report no.: Journal of the American Chemical Society
Abstract: 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.
URI: https://hdl.handle.net/10356/81713
http://hdl.handle.net/10220/39652
ISSN: 0002-7863
DOI: 10.1021/jacs.5b11014
Schools: School of Biological Sciences 
Rights: © 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.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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