(7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly
• 英文别名: MOCAc-Pro-Leu-Gly；2-[[(2S)-2-[[(2S)-1-[2-(7-methoxy-2-oxochromen-4-yl)acetyl]pyrrolidine-2-carbonyl]amino]-4-methylpentanoyl]amino]acetic acid
• 化学式: C₂₅H₃₁N₃O₈
• 分子量: 501.536
• InChiKey: IIEDBZTWPBXMRN-OALUTQOASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  36
• 可旋转键数：
  10
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.48
• 拓扑面积：
  151
• 氢给体数：
  3
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 在 calcium chloride Tris-HCl buffer 、 Bacillus themoproteolyticus thermolysin EC 3.4.24.27 、 sodium chloride 作用下， 以 二甲基亚砜 为溶剂， 生成 (7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly
  参考文献：
  名称：

  Substrate-dependent Activation of Thermolysin by Salt

  摘要：

  使用带正电荷的荧光底物(7-甲氧基香豆素-4-基)乙酰基-L-Pro-Leu-Gly-Leu-[N3-(2,4-二硝基苯基)-L-2,3-二氨基丙酰基]-L-Ala-L-Arg-NH2 [MOCAc-PLGL(Dpa)AR]检验了热溶解素的盐活化作用。热溶解酶的活性以双相指数方式增加，在有 4 M NaCl 存在时比没有 4 M NaCl 存在时高 40 倍。当[NaCl]o<0.5 M 和[NaCl]o>0.5 M 时，在 x M NaCl 下的活化程度分别为 4.7 倍和 2.3 倍。

  DOI：

  10.1271/bbb.68.1811

文献信息

• Inhibitory Effects of Lignans on the Activity of Human Matrix Metalloproteinase 7 (Matrilysin)
  作者：Yuko Muta、Sohei Oyama、Toshiaki Umezawa、Mikio Shimada、Kuniyo Inouye

  DOI：10.1021/jf049410n

  日期：2004.9.1

  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 muM. 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 muM), 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 metal loproteinases.