Active ester method is an efficient strategy to address the notorious racemization/epimerization issue of peptide bond formation. Herein, the pros and cons of using active esters for peptide synthesis were systematically summarized and analyzed.
We developed a stereoselective, racemization-free peptide bond formation method using Ns-protected FADIs, enabling fluoroalkene peptidomimetic synthesis with high stereochemical fidelity.
A TFPN-mediated esterification strategy enables the rapid synthesis of esters, thioesters, and macrolactones via in situ acyl fluorides. This process has a broad substrate scope and excellent functional group tolerance, as well as stereoretention.
Tissue transglutaminase (TG2) is both an enzyme and a G-protein that is implicated in many diseases, such that small molecule inhibitors of TG2 have broad potential as drugs or research tools.
A novel synthetic strategy for the construction of AviCys analogues via a highly efficient regio- and stereoselective hydrosulfuration of ynamides was reported.