192999-60-3

Upstream product

• 7364-51-4 N,O-bis(trimethylsilyl)phenylalanine 
• 192999-58-9 4-(phenylacetoxy)benzyl chloroformate 
• 63-91-2 L-phenylalanine 
• 192999-56-7 4-(hydroxymethyl)phenyl 2-phenylacetate 

Downstream Products

• 333362-91-7 N-phenylacetoxybenzyloxycarbonyl-L-alanyl-L-phenylalanyl-L-seryl-O-(3'-O-acetyl-6-N-allyloxycarbonyl-2'-deoxycytidyl-allyl-phosphato)-L-alanine allyl ester 
• 333362-89-3 N-phenylacetoxybenzyloxycarbonyl-L-phenylalanyl-L-seryl-O-(3'-O-acetyl-6-N-allyloxycarbonyl-2'-deoxycytidyl-allyl-phosphato)-L-alanine allyl ester 
• 333362-92-8 L-phenylalanyl-L-seryl-O-(3'-O-acetyl-6-N-allyloxycarbonyl-2'-deoxycytidyl-allyl-phosphato)-L-alanine allyl ester 
• 333362-87-1 N-phenylacetoxybenzyloxycarbonyl-L-phenylalanyl-L-seryl-L-alanine allyl ester 

Relevant academic research and scientific papers

Are PhAcOZ and Nsc suitable Nα-protecting groups for protease-catalysed peptide synthesis?

Protecting groups are necessary chemical tools in peptide synthesis. In protease-catalysed peptide synthesis they exert influence both on enzyme-substrate binding and on solubility. In this study, we have investigated the usability of various PhAcOZ- and Nsc-protected amino acids for protease-catalysed peptide synthesis. PhAcOZ-protected peptides were obtained in high yields using papain and thermolysin. In contrast to this, Nsc, as a base-labile ct-amino protecting group, is not suitable for biocatalytic synthesis under the conditions employed.

Chemoenzymatic synthesis of a characteristic phosphorylated and glycosylated peptide fragment of the large subunit of mammalian RNA polymerase II

The covalent modification of proteins by phosphorylation and addition of GlcNAc residues are important regulatory processes which mediate biological signal transduction. For instance, the cytosolic form of RNA polymerase II is heavily glycosylated but dur