5875-39-8

Usage

Uses

Used in Biochemistry and Pharmaceutical Research:
L-Serine, N-[(phenylmethoxy)carbonyl]-L-glutaminylis used as a building block for the synthesis of peptides and proteins, contributing to the development of new drugs and therapies.
Used in Therapeutic Applications:
L-Serine, N-[(phenylmethoxy)carbonyl]-L-glutaminylis used as a potential therapeutic agent for the treatment of various diseases and medical conditions, leveraging its properties to target specific biological processes and pathways.

Upstream product

• 32668-18-1 Z-Gln-Ser-OMe 
• 56-45-1 L-serin 
• 7763-16-8 N²-benzyloxycarbonyl-L-glutamine-(4-nitro-phenyl ester) 
• 2650-64-8 Cbz-L-Gln 

Relevant academic research and scientific papers

Discovery of potent and specific dihydroisoxazole inhibitors of human transglutaminase 2

Transglutaminase 2 (TG2) is a ubiquitously expressed enzyme that catalyzes the posttranslational modification of glutamine residues on protein or peptide substrates. A growing body of literature has implicated aberrantly regulated activity of TG2 in the pathogenesis of various human inflammatory, fibrotic, and other diseases. Taken together with the fact that TG2 knockout mice are developmentally and reproductively normal, there is growing interest in the potential use of TG2 inhibitors in the treatment of these conditions. Targeted-covalent inhibitors based on the weakly electrophilic 3-bromo-4,5-dihydroisoxazole (DHI) scaffold have been widely used to study TG2 biology and are well tolerated in vivo, but these compounds have only modest potency, and their selectivity toward other transglutaminase homologues is largely unknown. In the present work, we first profiled the selectivity of existing inhibitors against the most pertinent TG isoforms (TG1, TG3, and FXIIIa). Significant cross-reactivity of these small molecules with TG1 was observed. Structure-activity and -selectivity analyses led to the identification of modifications that improved potency and isoform selectivity. Preliminary pharmacokinetic analysis of the most promising analogues was also undertaken. Our new data provides a clear basis for the rational selection of dihydroisoxazole inhibitors as tools for in vivo biological investigation.

Peptide coupling of unprotected amino acids through in situ p-nitrophenyl ester formation

Several series of dipeptides and tripeptides were prepared via an activation-coupling method involving the in situ formation of a p-nitrophenyl ester of an (N-protected) amino acid, followed by coupling with an unprotected amino acid in partially aqueous solutions. The resulting peptide is easily isolated by precipitation. In general, the yields obtained are good to excellent and racemization is minimal. This method is particularly advantageous with respect to its simplicity and lack of obligatory side chain protection/deprotection steps.