Z-Leu-Leu-Glu-AMC peptide

Z-Leu-Leu-Glu-AMC peptide

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

Batch to batch variation of the purity

Cbz-LLE-AMC

Cbz-Leu-Leu-Glu-AMC

3

95.06%

C₃₅H₄₄N₄O₉

664.74

348086-66-8

25108642

Synthetic

Powder

The peptide Z-Leu-Leu-Glu-AMC is a fluorogenic substrate used to measure the proteolytic activity of the proteasome, specifically its caspase-like activity. This substrate is cleaved by the proteasome, resulting in the release of the fluorescent molecule 7-amino-4-methylcoumarin (AMC). By monitoring the fluorescence intensity, researchers can quantify the proteasome's activity, particularly its ability to cleave after acidic residues. This peptide is commonly used in studies related to protein degradation, such as those exploring neurodegenerative diseases like Parkinson's disease, where impaired proteasomal function is often implicated​.

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

• McNaught KS, Jenner P. Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci Lett. 2001 Jan 19;297(3):191-4. doi: 10.1016/s0304-3940(00)01701-8. PMID: 11137760.

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.