211990-57-7

Basic information

• Product Name: AC-IETD-AFC
• Synonyms: CASPASE 8 SUBSTRATE 1F, FLUOROGENIC;CASPASE-8 FLUOROGENIC SUBSTRATE;GRANZYME B SUBSTRATE I, COLORIMETRIC;AC-IETD-AFC;AC-ILE-GLU-THR-ASP-7-AMINO-4-TRIFLUORO-METHYLCOUMARIN;AC-ILE-GLU-THR-ASP-AFC;N-ACETYL-ILE-GLU-THR-ASP-(7-AMINO-4-TRIFLUOROMETHYLCOUMARIN);N-ACETYL-ILE-GLU-THR-ASP-7-AMINO-4-TRIFLUOROMETHYLCOUMARIN AFC
• CAS NO: 211990-57-7
• Molecular Formula: C31H38F3N5O12
• Molecular Weight: 729.65
• Product Categories: Caspases/Apoptosis;peptide;Caspase/Related Products
• Mol File: 211990-57-7.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 1113.8±65.0 °C(Predicted)
• Appearance: /
• Density: 1.437±0.06 g/cm3(Predicted)
• Storage Temp.: -20°C
• Solubility: Soluble in DMSO
• PKA: 4.09±0.10(Predicted)
• CAS DataBase Reference: AC-IETD-AFC(CAS DataBase Reference)
• NIST Chemistry Reference: AC-IETD-AFC(211990-57-7)
• EPA Substance Registry System: AC-IETD-AFC(211990-57-7)

Safety Data

• Hazardous Substances Data: 211990-57-7(Hazardous Substances Data)

Usage

Uses

Different sources of media describe the Uses of 211990-57-7 differently. You can refer to the following data:
1. N-Acetyl-Ile-Glu-Thr-Asp-7-amino-4-(trifluoromethyl)coumarin is a fluorogenic substrate for caspases -6, -8, and -10. The IETD sequence is based on the procaspase-3 cleavage site. Residues 172-175 of procaspase-3 are cleaved during apoptosis to produce the p12 subunit and a p20 peptide that is further cleaved to form the p17 subunit of mature caspase 3.
2. Ac-IETD-AFC is a fluorogenic substrate for caspase-8/caspase-3 processing enzyme and granzyme B. It is also a substrate for caspase-10. The IETD sequence is based on caspase-3 proenzyme cleavage site.

Downstream Products

• 53518-15-3 Coumarin 151 

Relevant articles and documents

Synthesis, enzymatic evaluation, and docking studies of fluorogenic caspase 8 tetrapeptide substrates

The synthesis, enzymatic evaluation, and molecular modeling studies of new fluorogenic tetrapeptide-based substrates selective for caspase 8, having the general structure Ac-IETD-AXX, are described. Various fluorescent reporter groups (AXX), i.e., 3- and 4-substituted coumarins and quinolin-2(1H)-ones were synthesized by von Pechmann condensation. They were subsequently coupled with the caspase-8-selective tetrapeptide Ac-IETD-OH under newly developed synthetic conditions to give the desired substrates in good yields and in high enantiomeric purity. Based on KM and Vmax values, the new compounds proved to be excellent substrates for recombinant human caspase 8. In contrast, the KM values for the same compounds as substrates for human caspase 3 were approximately 10-20-fold higher. Molecular modeling studies based on the X-ray crystal structures of both human caspases 3 and 8 revealed that there is sufficient room within both active sites to accommodate substrates with moderately bulky substituents in the 3- and 4-positions of the fluorogenic coumarins and quinolin-2(1H)-ones. Automated docking of the substrates into the active sites of both human caspases 3 and 8 with the program Auto-Dock 3 gave structures similar to the published crystallographic structures for the same tetrapeptide bound to caspase 8 in the form of an irreversible inhibitor. The calculated binding energies for the new substrates to either caspase 3 or 8 showed little difference between the substrates, consistent with the K M data. In addition, the calculated binding energies (ΔG) to caspase 8 were considerably more negative than those to caspase 3, also consistent with the KM data. A possible molecular interaction that might explain the selectivity of the IETD tetrapeptide motif for caspase 8 over caspase 3 is discussed.