Enzyme-Catalyzed Macrocyclization of Long Unprotected Peptides
Name
Pentelute_Enzyme-Catalyzed.pdf
Size
1.04 MB
Format
Adobe PDF
Checksum (MD5)
e3169accf1e92b5cf895c4d358190fd4
Author(s)
Zhang, Chi
Dai, Peng
Spokoyny, Alexander M.
Pentelute, Bradley L.
Date Issued
July 2014
Journal
Organic Letters
Publisher
American Chemical Society (ACS)
Citation
Zhang, Chi, Peng Dai, Alexander M. Spokoyny, and Bradley L. Pentelute. “Enzyme-Catalyzed Macrocyclization of Long Unprotected Peptides.” Organic Letters 16, no. 14 (July 18, 2014): 3652–3655.
Version
Final published version
Abstract
A glutathione S-transferase (GST) catalyzed macrocyclization reaction for peptides up to 40 amino acids in length is reported. GST catalyzes the selective SNAr reaction between an N-terminal glutathione (GSH, γ-Glu-Cys-Gly) tag and a C-terminal perfluoroaryl-modified cysteine on the same polypeptide chain. Cyclic peptides ranging from 9 to 24 residues were quantitatively produced within 2 h in aqueous pH = 8 buffer at room temperature. The reaction was highly selective for cyclization at the GSH tag, enabling the combination of GST-catalyzed ligation with native chemical ligation to generate a large 40-residue peptide macrocycle.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
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.
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1021/ol501609y
