Journal article
Aziridine-mediated ligation and site-specific modification of unprotected peptides
Journal of the American Chemical Society, Vol.133(50), pp.20033-20035
12/21/2011
Handle:
https://hdl.handle.net/2376/104508
PMID: 22112239
Abstract
A synthesis of aziridine-containing peptides via the Cu(II)-promoted coupling of unprotected peptide thioacids and N-H aziridine-2-carbonyl peptides is reported. The unique reactivity of the resulting N-acylated aziridine-2-carbonyl peptides facilitates their subsequent regioselective and stereoselective nucleophilic ring-opening to give unprotected peptides that are specifically modified at the ligation site. The aziridine-mediated peptide ligation concept is exemplified using H(2)O as the nucleophile, producing a Xaa-Thr linkage (where Xaa can be an epimerizable and hindered amino acid). The overall process is compatible with a variety of unprotected amino acid functionality, most notably the N-terminal and Lys side chain amines.
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Details
- Title
- Aziridine-mediated ligation and site-specific modification of unprotected peptides
- Creators
- Frank Brock Dyer - Department of Chemistry, Washington State University, Pullman, Washington 99164-4630, USAChung-Min ParkRyan JosephPhilip Garner
- Publication Details
- Journal of the American Chemical Society, Vol.133(50), pp.20033-20035
- Academic Unit
- Chemistry, Department of
- Publisher
- United States
- Identifiers
- 99900547080301842
- Language
- English
- Resource Type
- Journal article