1217265-50-3Relevant academic research and scientific papers
A mild and selective Pd-mediated methodology for the synthesis of highly fluorescent 2-arylated tryptophans and tryptophan-containing peptides: A catalytic role for Pd0 nanoparticles?
Williams, Thomas J.,Reay, Alan J.,Whitwood, Adrian C.,Fairlamb, Ian J. S.
, p. 3052 - 3054 (2014)
A Pd-mediated direct C-H bond functionalisation of tryptophan has been developed, both as a single amino acid residue and within peptides. Important mechanistic insight into this process has been gained by characterising a Pd catalytically competent nanoparticle phase which evolves during the early stages of reaction. The Royal Society of Chemistry.
Unified mild reaction conditions for C2-selective Pd-catalysed tryptophan arylation, including tryptophan-containing peptides
Reay, Alan J.,Williams, Thomas J.,Fairlamb, Ian J. S.
, p. 8298 - 8309 (2015/08/03)
Pd-mediated C-H bond functionalisation protocols have been designed and developed on tryptophan derivatives and tryptophan-containing peptides. The examination of different arylation reactions (three sets of different conditions A-C), all of which are notable for their low temperatures (≤40°C), allowed identification of unified and complementary synthetic approaches toward a series of functionalised tryptophan-containing products. Tryptophan-containing peptides demonstrated to be susceptible to aromatic oxidation were successfully and selectively modified through the application of diaryliodonium salts in good yields.
Postsynthetic modification of peptides: Chemoselective C-arylation of tryptophan residues
Ruiz-Rodriguez, Javier,Albericio, Fernando,Lavilla, Rodolfo
supporting information; experimental part, p. 1124 - 1127 (2010/06/14)
Born to be mild : The general, direct and selective C2 arylation of native Trp-containing peptides can be achieved by palladium-catalyzed C-H activation with aryl iodides in water, under microwave irradiation for a short time (see scheme). Under these mild conditions, the structural and stereochemical integrity of peptides is preserved.
