24629-22-9Relevant academic research and scientific papers
Chemoselective Peptide Backbone Diversification and Bioorthogonal Ligation by Ruthenium-Catalyzed C?H Activation/Annulation
Song, Liangliang,Ojeda-Carralero, Gerardo M.,Parmar, Divyaakshar,González-Martínez, David A.,Van Meervelt, Luc,Van der Eycken, Johan,Goeman, Jan,Rivera, Daniel G.,Van der Eycken, Erik V.
supporting information, p. 3297 - 3304 (2021/05/11)
The field of peptide derivatization by metal-catalyzed C?H activation has been mostly directed to modify the side chains, but poor attention has been given to the peptide backbone. Here we report a ruthenium-catalyzed C?H activation/annulation process that can chemoselectively modify the peptide backbone producing functionalized isoquinolone scaffolds with high regioselectivity in a rapid and step-economical manner. This strategy is characterized by racemization-free conditions and the production of fluorescent peptides, and peptide conjugates to drugs, natural products and other peptide fragments, providing a chemical approach for the construction of novel peptide-pharmacophore conjugates. Mechanistic studies suggest that amide bonds of peptide backbone act as the bidentate directing group to promote the C?H activation/annulation process. This report provides an unprecedented example of peptide backbone diversification and bioorthogonal ligation exploiting the power of ruthenium-catalyzed C?H activation. (Figure presented.).
Chemical protein synthesis by kinetically controlled ligation of peptide O-esters
Zheng, Ji-Shen,Cui, Hong-Kui,Fang, Ge-Min,Xi, Wei-An,Liu, Lei
scheme or table, p. 511 - 515 (2010/12/25)
(Chemical Equation Presented) Designer peptides: A large reactivity difference was observed between two peptide O-esters that can undergo peptide ligation through an situ O-to-S acyl shift. This observation allowed the designed of "one-pot" N-to-C sequential peptide fragment condensation through kinetically controlled ligation with more readily accessible peptide O-esters.
