929294-62-2Relevant academic research and scientific papers
Solid-phase synthesis of Stat3 inhibitors incorporating O-carbamoylserine and O-carbamoylthreonine as glutamine mimics
Mandal, Pijus K.,Heard, Patricia A.,Ren, Zhiyong,Chen, Xiaomin,McMurray, John S.
, p. 654 - 656 (2007)
O-Carbamoylserine and O-carbamoylthreonine are glutamine analogues that were incorporated into a Stat3 inhibitory peptide to probe the requirements of Gln at the pY+3 position. Fmoc-Ser-NHBn and Fmoc-Thr-NHBn were converted to nitrophenyl carbonates and were attached to Rink resin via a side-chain carbamate linkage. After assembly of the peptide, acid treatment resulted in O-carbamoylserine and O-carbamoylthreonine-containing peptides. The order of affinity for Stat3 was Gln > Ser(CONH2) ? Thr(CONH2) suggesting a relatively tight binding pocket for the side chain of glutamine.
Aziridine-mediated ligation and site-specific modification of unprotected peptides
Dyer, Frank Brock,Park, Chung-Min,Joseph, Ryan,Garner, Philip
supporting information; experimental part, p. 20033 - 20035 (2012/01/31)
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 t
