140430-56-4

Basic information

• Product Name: MOCAC-PRO-LEU-GLY
• Synonyms: MOCAC-PRO-LEU-GLY;7-METHOXYCOUMARIN-4-ACETYL-PRO-LEU-GLY;(7-METHOXYCOUMARIN-4-YL)ACETYL-L-PROLYL-L-LEUCYLGLYCINE
• CAS NO: 140430-56-4
• Molecular Formula: C25H31N3O8
• Molecular Weight: 501.53
• Mol File: 140430-56-4.mol

Chemical Properties

• Appearance: /
• Storage Temp.: −20°C
• CAS DataBase Reference: MOCAC-PRO-LEU-GLY(CAS DataBase Reference)
• NIST Chemistry Reference: MOCAC-PRO-LEU-GLY(140430-56-4)
• EPA Substance Registry System: MOCAC-PRO-LEU-GLY(140430-56-4)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 140430-56-4(Hazardous Substances Data)

Relevant articles and documents

Substrate-dependent activation of thermolysin by salt

Salt-activation of thermolysin was examined using a positively charged fluorescent substrate, (7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu- [N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH 2 [MOCAc-PLGL(Dpa)AR]. Thermolysin activity increased in a biphasic exponential fashion and was 40 times higher in the presence of 4 M NaCl than in its absence. The degree of activation at X M NaCl was expressed as 4.7 x when [NaCl]0 x when [NaCl]0 > 0.5 M respectively.

Inhibitory effect of lignans on the activity of human matrix metalloproteinase 7 (matrilysin)

Inhibitory effects of nine dibenzylbutyrolactone lignans on a human matrix metalloproteinase, matrilysin, were examined. All of the lignans examined inhibited matrilysin with the IC50 values ranging from 50 to >280 μM. Matairesinol, which has the basic structure of the other lignans, showed the weakest inhibition. Lignans with methylenedioxy ring(s) or a hydroxyl group at the C5-position inhibited matrilysin more strongly than matairesinol. 5-Hydroxypluviatolide, which has both a methylenedioxy ring and a hydroxyl group at the C5-position, was the most potent inhibitor (IC50 = 50 μM), suggesting that the introduction of these two elements might enhance synergistically the inhibitory activity of lignans. 5-Hydroxypluviatolide inhibited matrilysin in a competitive manner, and its inhibitory effect was greatly suppressed by the presence of another competitive inhibitor, dimethyl sulfoxide. The precursors of matairesinol, coniferyl alcohol and secoisolariciresinol, had no inhibitory activity, indicating that the dibenzylbutyrolactone structure is essential for the inhibition. It has been shown that lignans have the potential to inhibit matrilysin, and the knowledge of their structure-activity relationship might be beneficial to developing selective inhibitors for matrix metalloproteinases.

Effects of salts on the interaction of 8-anilinonaphthalene 1-sulphonate and thermolysin

Neutral salts activate and stabilize thermolysin. In this study, to explore the mechanism, we analyzed the interaction of 8-anilinonaphthalene 1-sulphonate (ANS) and thermolysin by ANS fluorescence. At pH 7.5, the fluorescence of ANS increased and blue-shifted with increasing concentrations (0-2.0 μM) of thermolysin, indicating that the anilinonaphthalene group of ANS binds with thermolysin through hydrophobic interaction. ANS did not alter thermolysin activity. The dissociation constants (Kd) of the complex between ANS and thermolysin was 33 ± 2 μM at 0 M NaCl at pH 7.5, decreased with increasing NaCl concentrations, and reached 9 ± 3 μM at 4M NaCl. The Kd values were not varied (31-34 μM) in a pH range of 5.5-8.5. This suggests that at high NaCl concentrations, Na+ and/or Cl- ions bind with thermolysin and affect the binding of ANS with thermolysin. Our results also suggest that the activation and stabilization of thermolysin by NaCl are partially brought about by the binding of Na+ and/or Cl- ions with thermolysin.