18538-27-7Relevant articles and documents
Application of High-Throughput Competition Experiments in the Development of Aspartate-Directed Site-Selective Modification of Tyrosine Residues in Peptides
Chinn, Alex J.,Hwang, Jaeyeon,Kim, Byoungmoo,Parish, Craig A.,Krska, Shane W.,Miller, Scott J.
supporting information, p. 9424 - 9433 (2020/08/14)
Herein we report a Cu-catalyzed, site-selective functionalization of peptides that employs an aspartic acid (Asp) as a native directing motif, which directs the site of O-arylation at a proximal tyrosine (Tyr) residue. Through a series of competition studies conducted in high-throughput reaction arrays, effective conditions were identified that gave high selectivity for the proximal Tyr in Asp-directed Tyr modification. Good levels of site-selectivity were achieved in the O-arylation at a proximal Tyr residue in a number of cases, including a peptide-small molecule hybrid.
