14281-55-1Relevant articles and documents
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.).
3-AMINOACYL-TETRAHYDROTHIAZOLE-2-THIONE AS AN ACTIVE AMIDE FOR PEPTIDE SYNTHESIS (I)
Chung-hsi, Li,Yuen-hwa, Yieh,Yao, Lin,Yong-jun, Lu,Ai-hsueh, Chi,Chi-yi, Hsing
, p. 3467 - 3470 (2007/10/02)
3-Aminoacyl-tetrahydrothiazole-2-thione can be used as an active amide for peptide synthesis.A series of peptides have been synthesized with satisfactory yields by this methods.
