201852-70-2

Basic information

• Product Name: H-GLY-PHE-AMC
• Synonyms: GLYCYL-L-PHENYLALANINE 7-AMIDO-4-METHYLCOUMARIN;GLYCYL-L-PHENYLALANINE AMC;GLY-PHE-7-AMINO-4-METHYLCOUMARIN;GLY-PHE-AMC;H-GLY-PHE-AMC
• CAS NO: 201852-70-2
• Molecular Formula: C₂₁H₂₁N₃O₄
• Molecular Weight: 379.41
• Mol File: 201852-70-2.mol

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: H-GLY-PHE-AMC(CAS DataBase Reference)
• NIST Chemistry Reference: H-GLY-PHE-AMC(201852-70-2)
• EPA Substance Registry System: H-GLY-PHE-AMC(201852-70-2)

Safety Data

• Hazardous Substances Data: 201852-70-2(Hazardous Substances Data)

Upstream product

• 26093-31-2 7-amino-4-methylcoumarin. 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 110625-79-1 tert-butyl (S)-(1-((4-methyl-2-oxo-2H-chromen-7-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 98516-72-4 H-Phe-NH-Mec 
• 35661-40-6 N-Fmoc L-Phe 

Downstream Products

• 3321-03-7 Gly-Phe-OH 

Relevant articles and documents

Development of the first internally-quenched fluorescent substrates of human cathepsin C: The application in the enzyme detection in biological samples

Cathepsin C is a widely expressed cysteine exopeptidase that is mostly recognized for the activation of the granule-associated proinflammatory serine proteases in neutrophils, cytotoxic T lymphocytes and mast cells. It has been shown that the enzyme can be secreted extracellularly; however, its occurrence in human bodily fluids/physiological samples has not been thoroughly studied. In the course of this study, the first fluorescence resonance energy transfer peptides for the measurement of the activity of human cathepsin C were designed and synthesized. Two series of tetra- and pentapeptide substrates enabled the detailed S′ specificity study of cathepsin C, which has been examined for the first time. The extensive enzymatic studies of the obtained compounds resulted in the selection of the highly specific and selective substrate Thi-Ala(Mca)-Ser-Gly-Tyr(3-NO2)-NH2, which was successfully employed for the detection of cathepsin C activity in complex biological samples such as cell lysates, urine and bronchoalveolar lavage fluids. Molecular docking of the selected substrate was performed in order to better understand the binding mode of the substrates in the active site of cathepsin C.

A judgment on postmortem aging in Longissimus dorsi based on a peptide substrate library

We attempted to develop a method to determine easily and effectively the degree of postmortem aging of pork longissimus dorsi (LD) by measuring the activity of proteases in the LD using fluorogenic peptide substrates. LD was used to measure the change with time in the protease activity detected with these substrates. Determining the variations within the LD muscles, strong positive correlations were found between changes in hardness and fluorescence intensities against Ac-Ala-MCA, Ac-Met-MCA, Ac-Ser-MCA, Ac-Thr-MCA, and Ac-Ala-Phe-MCA (P 0.005), and strong negative correlations were found between changes in total amounts of free amino acids and Ac-Ala-MCA, Ac-Met-MCA, Ac-Ser-MCA, Ac-Thr-MCA, and Ac-Ala-Phe-MCA (P 0.001). Negative correlations were also observed between changes in the amounts of free Ala, Arg, Lys, Leu, Met, Phe, and Tyr and the fluorescence intensities against Ala, Arg, Lys, Leu, Met, Phe, and Tyr-MCA respectively (P 0.001).