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.
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.
We report a chemoselective amide coupling strategy that selectively reacts with hindered amine in the presence of competing primary alcohols and amines with excellent chemoselectivity, reactivity, and minimal epimerization.
The mechanochemical protecting-group-free amidation of hydroxycarboxylic acids is presented. The transformation is applied to the synthesis of imatinib via a two-fold C–N bond construction sequence that bypasses a chlorinated genotoxic intermediate.