Protein Thioester Synthesis Enabled by Sortase
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Pentelute_Protein thioester.pdf
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943.47 KB
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Author(s)
Ling, Jingjing
Policarpo, Rocco L.
Rabideau, Amy E.
Liao, Xiaoli
Pentelute, Bradley L.
Date Issued
July 2012
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society
Citation
Ling, Jingjing J., Rocco L. Policarpo, Amy E. Rabideau, Xiaoli Liao, and Bradley L. Pentelute. “Protein Thioester Synthesis Enabled by Sortase.” Journal of the American Chemical Society 134, no. 26 (July 4, 2012): 10749-10752.
Version
Author's final manuscript
Abstract
Proteins containing a C-terminal thioester are important intermediates in semisynthesis. Currently there is one main method for the synthesis of protein thioesters that relies upon the use of engineered inteins. Here we report a simple strategy, utilizing sortase A, for routine preparation of recombinant proteins containing a C-terminal αthioester. We used our method to prepare two different anthrax toxin cargo proteins: one containing an αthioester and another containing a D-polypeptide segment situated between two protein domains. We show that both variants can translocate through protective antigen pore. This new method to synthesize a protein thioester allows for interfacing of sortase-mediated ligation and native chemical ligation.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1021/ja302354v
