Journal
ORGANIC LETTERS
Volume 18, Issue 5, Pages 1186-1189Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.orglett.6b00317
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Funding
- University Research Council (URC)
- NASA NJ Space Grant Consortium
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Site-specific hydrolysis of peptide bonds at glutamic acid under neutral aqueous conditions is reported. The method relies on the activation of the backbone amide chain at glutamic acid by the formation of a pyroglutamyl (pGlu) imide moiety. This activation increases the susceptibility of a peptide bond toward hydrolysis. The method is highly specific and demonstrates broad substrate scope including cleavage of various bioactive peptides with unnatural amino acid residues, which are unsuitable substrates for enzymatic hydrolysis.
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