130380-48-2Relevant academic research and scientific papers
Comparative lipase-catalyzed hydrolysis of ethylene glycol derived esters. The 2-methoxyethyl ester as a protective group in peptide and glycopeptide synthesis
Gewehr, Markus,Kunz, Horst
, p. 1499 - 1510 (2007/10/03)
Comparison of the lipase-catalyzed cleavage of polar esters derived from ethylene glycol proved 2-methoxyethyl (ME) esters most favorable protecting groups for the carboxylic function of peptides and glycopeptides. They combine high substrate acceptance and iligh yields of hydrolysis with favorable physicochemical properties and advantageous solubility. The application of this polar ester as protecting group was extended to N-glycosylated amino acids and N-glycopeptides. The selective removal of ME esters by lipases was achieved under mild conditions (pH 7.0 and 37°C), leaving all other linkages including peptide bonds and other ester protecting groups unaffected.
Selective Enzymatic Removal of Protecting Groups: n-Heptyl Esters as Carboxy Protecting Functions in Peptide Synthesis
Braun, Peter,Waldmann, Herbert,Vogt, Walter,Kunz, Horst
, p. 165 - 170 (2007/10/02)
Amino acid heptyl (Hep) esters are accessible as generally crystalline hydro tosylates 3 from the amino acids by azeotropic esterification with 1-heptanol in high yields.They can be condensed with Z-, Boc-, and Aloc-protected amino acids to give the dipep
