Z-GPR-AMC peptide

Z-GPR-AMC peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

Cbz-GPR-AMC

Cbz-Gly-Pro-Arg-AMC

3

95.28%

C₃₁H₃₇N₇O₇

619.67

Synthetic

Powder

The peptide Z-GPR-AMC (benzyloxycarbonyl-glycine-proline-arginine-7-amino-4-methylcoumarin) is a fluorogenic substrate commonly used to measure the proteolytic activity of enzymes, particularly cathepsin K. Upon enzymatic cleavage, the 7-amino-4-methylcoumarin (AMC) is released, which fluoresces and allows quantification of enzymatic activity. This substrate is especially useful in studies involving cysteine proteases like cathepsins, and it has been applied in the study of diseases such as osteoporosis, cancer metastasis, and atherosclerosis. Z-GPR-AMC is considered specific for cathepsin K but can also be hydrolyzed to some extent by other cathepsins, such as cathepsin B. Its use is often paired with inhibitors like CA-074 to prevent cross-reactivity with cathepsin B, ensuring more accurate measurements of cathepsin K activity.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual: Handling and Storage of Synthetic Peptides

• Li WA, Barry ZT, Cohen JD, Wilder CL, Deeds RJ, Keegan PM, Platt MO. Detection of femtomole quantities of mature cathepsin K with zymography. Anal Biochem. 2010 Jun 1;401(1):91-8. doi: 10.1016/j.ab.2010.02.035. Epub 2010 Mar 3. PMID: 20206119.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.