1634-89-5

Usage

Uses

Used in Pharmaceutical Industry:
Z-GLU-GLY-OH is used as a building block in peptide synthesis for the development of new pharmaceuticals. Its protecting group allows for controlled synthesis of complex peptide structures, which is crucial for creating effective drug molecules.
Used in Research and Development:
In the field of research, Z-GLU-GLY-OH is utilized as a model compound for studying protein structure and function. Its unique properties enable scientists to investigate the interactions between amino acids and other biomolecules, contributing to a better understanding of biological processes.
Used in Drug Design:
Z-GLU-GLY-OH is employed as a component in the design of drugs targeting specific biological pathways. Its potential biological activities and pharmacological properties are being explored to develop new therapeutic agents for various diseases.
Used in Biochemistry Education:
In educational settings, Z-GLU-GLY-OH serves as a practical example for teaching the principles of peptide synthesis and the role of protecting groups in organic chemistry and biochemistry. This helps students grasp the concepts of drug development and protein structure analysis.

InChI:InChI=1/C15H18N2O7/c18-12(19)7-6-11(14(22)16-8-13(20)21)17-15(23)24-9-10-4-2-1-3-5-10/h1-5,11H,6-9H2,(H,16,22)(H,17,23)(H,18,19)(H,20,21)

Upstream product

• 56-40-6 glycine 
• 27565-41-9 1,4-dithio-D,L-threitol 
• 13139-17-8 N-(Benzyloxycarbonyloxy)succinimide 
• 133464-46-7 (S)-2-[((9H-fluoren-9-yl)methoxy)carbonylamino]-5-(allyloxy)-5-oxopentanoic acid 
• 25126-07-2 N-(benzyloxycarbonyl)-L-glutamic acid, α-phenyl ester 
• 4587-39-7 N-Benzyloxycarbonyl-α-L-glutamylglycin-ethylester-γ-phenylhydrazid 
• 1155-62-0 N-benzyloxycarbonyl-L-glutamic acid 
• 5672-83-3 Z-L-GluOMe 
• 17219-65-7 glycine hydrobromide 
• 30960-05-5 (S)-4-(((benzyloxy)carbonyl)amino)-5-((2-(tert-butoxy)-2-oxoethyl)amino)-5-oxopentanoic acid 
• 908571-04-0 N-[N-(N-benzyloxycarbonyl-α-L-glutamyl)-glycyl]-glycine 
• 89714-94-3 acetic acid-[(25R)-5α-spirosta-7,9(11)-dien-3β-yl ester 
• 4587-40-0 N-(N-benzyloxycarbonyl-α-L-glutamyl)-glycine ethyl ester 
• 15149-57-2 Z-L-Glu(OEt)-Gly-OEt 

Downstream Products

• 1155-62-0 N-benzyloxycarbonyl-L-glutamic acid 
• 13716-89-7 Glu-Gly 

Relevant academic research and scientific papers

Synthesis and Kinetic Characterisation of Water-Soluble Fluorogenic Acyl Donors for Transglutaminase 2

Small glutamate-containing peptides bearing coumarin derivatives as fluorescent leaving groups attached to the γ-carboxylic acid group of the Glu residue were synthesised and investigated with regard to their potential to act as substrates for transglutam

MODIFICATION OF ENZYMATIC CROSSLINKERS FOR CONTROLLING PROPERTIES OF CROSSLINKED MATRICES

Improved matrix or hydrogel that is formed by enzymatic crosslinking of polymers wherein the crosslinking enzyme molecules have been modified for the purpose of improving the crosslinking density, mechanical properties, or other properties of the matrix, and/or to provide improved control over the rate and/or extent of crosslinking, wherein the enzyme molecules are modified to alter the perceived volume of the enzyme molecules in the crosslinked matrix being formed. Methods of production and of use are also provided.

Acyl transfer from carboxylate, carbonate, and thiocarbonate esters to enzymatic and nonenzymatic thiolates

Transglutaminases (EC 2.3.2.13) (TGases) catalyze calcium-dependent acyl transfer reactions between peptide-bound glutamine residues as acyl donors and peptide-bound lysine residues as acyl acceptors, resulting in the formation of intermolecular ε-(γ-glutamyl)lysine crosslinks. The mechanistic details of its "ping-pong" transamidation reaction remain unknown. In particular, few studies have been published probing the nucleophilicity of TGase using acyl-donor substrates of varied electrophilicity. Herein we report the synthesis of activated esters of carbonates, carbamates, and thiocarbonates and their reactions with simple thiols, as a nonenzymatic point of reference, and with the catalytic cysteine residue of guinea pig liver TGase. Our kinetic results show that the simple substitution of a side chain methylene unit by oxygen or sulphur had a surprising effect on both substrate affinity and acylation reactivity. Furthermore, they provide unexpected insight into the importance of a side chain heteroatom for conferring affinity for tissue TGase as well as revealing an interesting class of irreversible inhibitors.

V8 PROTEINASE-CATALYZED PEPTIDE SYNTHESIS IN HYDROPHILIC ORGANIC SOLVENTS WITH LOW WATER CONTENT

Free Staphylococcus aureus V8 proteinase was applied to coupling reactions of Z-Glu-OMe, Z-Glu-OBzl, Z-Ala-Glu-OMe, and Z-Ala-Ala-Glu-OMe with various amino acid amides and peptides in acetonitrile containing 5 vol. percent of water.No synthesis of Z-Asp-Leu-NH2 was achieved under the same conditions.The synthesis of Z-Glu-Leu-NH2 proceeded analogously also in 2-propanol or tert-butanol.