《Application of high-throughput competition experiments in the development of aspartate-directed site-selective modification of tyrosine residues in peptides》 was written by Chinn, Alex J.; Hwang, Jaeyeon; Kim, Byoungmoo; Parish, Craig A.; Krska, Shane W.; Miller, Scott J.. Recommanded Product: 5781-53-3 And the article was included in Journal of Organic Chemistry in 2020. The article conveys some information:
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 mol. hybrid.Methyl 2-chloro-2-oxoacetate(cas: 5781-53-3Recommanded Product: 5781-53-3) was used in this study.
Methyl 2-chloro-2-oxoacetate(cas: 5781-53-3) belongs to acyl chlorides. Lacking the ability to form hydrogen bonds, acyl chlorides have lower boiling and melting points than similar carboxylic acids. For example, acetic acid boils at 118 °C, whereas acetyl chloride boils at 51 °C. Like most carbonyl compounds, infrared spectroscopy reveals a band near 1750 cm−1.Recommanded Product: 5781-53-3
Referemce:
Chloride – Wikipedia,
Chlorides – an overview | ScienceDirect Topics