2-[[1-adamantyloxy-[1-(9H-fluoren-9-ylmethoxycarbonylamino)-2-phenylethyl]phosphoryl]methyl]-5-phenylpentanoic acid | 237394-58-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: 2-[[1-adamantyloxy-[1-(9H-fluoren-9-ylmethoxycarbonylamino)-2-phenylethyl]phosphoryl]methyl]-5-phenylpentanoic acid
• CAS: 237394-58-0
• 化学式: C₄₅H₅₀NO₆P
• 分子量: 731.869
• InChiKey: NAXDHZAPGWEXKZ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  9.4
• 重原子数：
  53
• 可旋转键数：
  16
• 环数：
  9.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  102
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  4,6-二氯吲哚-2-甲酸 、 、 2-[[1-adamantyloxy-[1-(9H-fluoren-9-ylmethoxycarbonylamino)-2-phenylethyl]phosphoryl]methyl]-5-phenylpentanoic acid 生成 [2-[[(2S)-1-amino-3-(1H-indol-3-yl)-1-oxopropan-2-yl]carbamoyl]-5-phenylpentyl]-[1-[(4,6-dichloro-1H-indole-2-carbonyl)amino]-2-phenylethyl]phosphinic acid
  参考文献：
  名称：

  Phosphinic Pseudo-Tripeptides as Potent Inhibitors of Matrix Metalloproteinases:  A Structure−Activity Study

  摘要：

  Several phosphinic pseudo-tripeptides of general formula R-Xaa Psi (PO2-CH2)Xaa'-Yaa'-NH2 were synthesized and evaluated for their in vitro activities to inhibit stromelysin-3, gelatinases A and B, membrane type-1 matrix metalloproteinase, collagenases 1 and 2, and matrilysin. With the exception of collagenase-1 and matrilysin, phosphinic pseudo-tripeptides behave as highly potent inhibitors of matrix metalloproteinases, provided they contain in P-1' position an unusual long aryl-alkyl substituent. Study of structure-activity relationships regarding the influence of the R and Xaa' substituents in this series may contribute to the design of inhibitors able to block only a few members of the matrix metalloproteinase family.

  DOI：

  10.1021/jm9900164
• 作为产物：
  描述：

  (2-Ethoxycarbonyl-5-phenylpentyl)-[2-phenyl-1-(phenylmethoxycarbonylamino)ethyl]phosphinic acid 在 palladium on activated charcoal sodium hydroxide 、 ammonium formate 、 sodium carbonate 、 silver(l) oxide 作用下， 以 1,4-二氧六环 、 甲醇 、 氯仿 为溶剂， 反应 24.7h， 生成 2-[[1-adamantyloxy-[1-(9H-fluoren-9-ylmethoxycarbonylamino)-2-phenylethyl]phosphoryl]methyl]-5-phenylpentanoic acid
  参考文献：
  名称：

  Phosphinic Pseudo-Tripeptides as Potent Inhibitors of Matrix Metalloproteinases:  A Structure−Activity Study

  摘要：

  Several phosphinic pseudo-tripeptides of general formula R-Xaa Psi (PO2-CH2)Xaa'-Yaa'-NH2 were synthesized and evaluated for their in vitro activities to inhibit stromelysin-3, gelatinases A and B, membrane type-1 matrix metalloproteinase, collagenases 1 and 2, and matrilysin. With the exception of collagenase-1 and matrilysin, phosphinic pseudo-tripeptides behave as highly potent inhibitors of matrix metalloproteinases, provided they contain in P-1' position an unusual long aryl-alkyl substituent. Study of structure-activity relationships regarding the influence of the R and Xaa' substituents in this series may contribute to the design of inhibitors able to block only a few members of the matrix metalloproteinase family.

  DOI：

  10.1021/jm9900164

文献信息

• Phosphinic Pseudo-Tripeptides as Potent Inhibitors of Matrix Metalloproteinases:  A Structure−Activity Study
  作者：Stamatia Vassiliou、Artur Mucha、Philippe Cuniasse、Dimitris Georgiadis、Karine Lucet-Levannier、Fabrice Beau、Rama Kannan、Gillian Murphy、Vera Knäuper、Marie-Christine Rio、Paul Basset、Athanasios Yiotakis、Vincent Dive

  DOI：10.1021/jm9900164

  日期：1999.7.1

  Several phosphinic pseudo-tripeptides of general formula R-Xaa Psi (PO2-CH2)Xaa'-Yaa'-NH2 were synthesized and evaluated for their in vitro activities to inhibit stromelysin-3, gelatinases A and B, membrane type-1 matrix metalloproteinase, collagenases 1 and 2, and matrilysin. With the exception of collagenase-1 and matrilysin, phosphinic pseudo-tripeptides behave as highly potent inhibitors of matrix metalloproteinases, provided they contain in P-1' position an unusual long aryl-alkyl substituent. Study of structure-activity relationships regarding the influence of the R and Xaa' substituents in this series may contribute to the design of inhibitors able to block only a few members of the matrix metalloproteinase family.