5-(dibenzylphosphono)valeric acid | 474644-26-3

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机膦酸及其衍生物
• 英文名称: 5-(dibenzylphosphono)valeric acid
• 英文别名: 5-(dibenzylphosphonyl)pentanoic acid；5-Bis(phenylmethoxy)phosphorylpentanoic acid
• CAS: 474644-26-3
• 化学式: C₁₉H₂₃O₅P
• 分子量: 362.362
• InChiKey: IZEOXXIBHJZRTA-UHFFFAOYSA-N

物化性质

• 沸点：
  550.1±50.0 °C(Predicted)
• 密度：
  1.220±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  25
• 可旋转键数：
  11
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  72.8
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  5-(dibenzylphosphono)valeric acid 在 叠氮磷酸二苯酯 、 三乙胺 作用下， 以 乙醇 、 甲苯 为溶剂， 生成 9H-fluoren-9-ylmethyl N-[4-bis(phenylmethoxy)phosphorylbutylcarbamoylamino]carbamate
  参考文献：
  名称：

  用于金属氧化物和沸石纳米颗粒功能化的氨基脲基膦酸的合成

  摘要：

  描述了具有 Fmoc 保护的氨基脲基团的两种膦酸的合成。关键步骤是在二苄基膦酸酯存在下进行的 Curtius 重排。初步实验表明，膦酸可以接枝在氧化物纳米粒子和胶体沸石纳米晶体的表面，而无需对 Fmoc 基团进行脱保护。

  DOI：

  10.1055/s-2004-829565
• 作为产物：
  描述：

  亚磷酸二苄酯 在 lithium hydroxide 、 sodium hydride 作用下， 以 四氢呋喃 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 26.25h， 生成 5-(dibenzylphosphono)valeric acid
  参考文献：
  名称：

  Incorporation of an Amide into 5-Phosphonoalkyl-6-d-ribitylaminopyrimidinedione Lumazine Synthase Inhibitors Results in an Unexpected Reversal of Selectivity for Riboflavin Synthase vs Lumazine Synthase

  摘要：

  Several analogues of a hypothetical intermediate in the reaction catalyzed by lumazine synthase were synthesized and tested as inhibitors of both Bacillus subtilis lumazine synthase and Escherichia coli riboflavin synthase. The new compounds were designed by replacement of a two-carbon fragment of several 5-phosphonoalkyl-6-D-ribitylaminopyrimidinedione lumazine synthase inhibitors with an amide linkage that was envisioned as an analogue of a Schiff base moiety of a hypothetical intermediate in the enzyme-catalyzed reaction. The incorporation of the amide group led to an unexpected reversal in selectivity for inhibition of lumazine synthase vs riboflavin synthase. Whereas the parent 5-phosphonoalkyl-6-D-ribitylaminopyrimidinediones were lumazine synthase inhibitors and did not inhibit riboflavin synthase, the amide-containing derivatives inhibited riboflavin synthase and were only very weak or inactive as lumazine synthase inhibitors. Molecular modeling of inhibitor-lumazine synthase complexes did not reveal a structural basis for these unexpected findings. However, molecular modeling of one of the inhibitors with E. coli riboflavin synthase demonstrated that the active site of the enzyme could readily accommodate two ligand molecules.

  DOI：

  10.1021/jo020144r

文献信息

• Isoprenoid Biosynthesis via the Methylerythritol Phosphate Pathway: Structural Variations around Phosphonate Anchor and Spacer of Fosmidomycin, a Potent Inhibitor of Deoxyxylulose Phosphate Reductoisomerase
  作者：Catherine Zinglé、Lionel Kuntz、Denis Tritsch、Catherine Grosdemange-Billiard、Michel Rohmer

  DOI：10.1021/jo9024732

  日期：2010.5.21

  Fosmidomycin and its analogue FR-900098 are potent inhibitors of 1-deoxy-d-xylulose 5-phosphate reducto-isomerase (DXR), the second enzyme of the MEP pathway for the biosynthesis of isoprenoids. This paper describes the synthesis of analogues of the two reverse phosphonohydroxamic acids 3 and 4, in which the length of the carbon spacer is modified, the N-methyl group of 3 is replaced by an ethyl group

  膦胺霉素和其类似物FR-900098是1-脱氧的有效抑制剂d -xylulose -5-磷酸粉身碎骨异构酶（DXR），为类异戊二烯的生物合成的MEP途径的第二种酶。本文描述的两个倒phosphonohydroxamic酸类似物的合成3和4，其中，所述碳间隔的长度被修改，Ñ甲基组3是由乙基取代，和磷酸基团通过取代的潜在等位部分，即磺酸盐或羧酸盐官能团。评价了合成的类似物抑制大肠杆菌DXR的潜力。
• [EN] N-SUBSTITUTED INDOLE DERIVATIVES AND CONJUGATES FOR THE TREATMENT OF CANCER<br/>[FR] DÉRIVÉS D'INDOLES N-SUBSTITUÉS ET CONJUGUÉS POUR LE TRAITEMENT DU CANCER
  申请人：[en]DIACCURATE

  公开号：WO2024003002A1

  公开（公告）日：2024-01-04

  The present invention relates to N-substituted derivatives of indoles of formula (I): and their use in the treatment of cancer. The invention further provides protein-drug conjugates, more particularly antibody-drug conjugates, from compounds of formula (I).
• Synthesis of Phosphonic Acids with the Semicarbazide Group for the Functionalization of Metal Oxide and Zeolite Nanoparticles
  作者：Tristan Doussineau、Jean-Olivier Durand、Michel Granier、Monique Smaïhi、Valentin Valtchev

  DOI：10.1055/s-2004-829565

  日期：——

  The syntheses of two phosphonic acids possessing the Fmoc-protected semicarbazide group are described. The key step was the Curtius rearrangement, performed in the presence of dibenzyl phosphonate esters. Preliminary experiments showed that the phosphonic acid can be grafted at the surface of oxide nanoparticles and colloidal zeolite nanocrystals, without deprotection of the Fmoc group.

  描述了具有 Fmoc 保护的氨基脲基团的两种膦酸的合成。关键步骤是在二苄基膦酸酯存在下进行的 Curtius 重排。初步实验表明，膦酸可以接枝在氧化物纳米粒子和胶体沸石纳米晶体的表面，而无需对 Fmoc 基团进行脱保护。
• Incorporation of an Amide into 5-Phosphonoalkyl-6-<scp>d</scp>-ribitylaminopyrimidinedione Lumazine Synthase Inhibitors Results in an Unexpected Reversal of Selectivity for Riboflavin Synthase vs Lumazine Synthase
  作者：Mark Cushman、Donglai Yang、Jeffrey T. Mihalic、Jinhua Chen、Stefan Gerhardt、Robert Huber、Markus Fischer、Klaus Kis、Adelbert Bacher

  DOI：10.1021/jo020144r

  日期：2002.10.1

  Several analogues of a hypothetical intermediate in the reaction catalyzed by lumazine synthase were synthesized and tested as inhibitors of both Bacillus subtilis lumazine synthase and Escherichia coli riboflavin synthase. The new compounds were designed by replacement of a two-carbon fragment of several 5-phosphonoalkyl-6-D-ribitylaminopyrimidinedione lumazine synthase inhibitors with an amide linkage that was envisioned as an analogue of a Schiff base moiety of a hypothetical intermediate in the enzyme-catalyzed reaction. The incorporation of the amide group led to an unexpected reversal in selectivity for inhibition of lumazine synthase vs riboflavin synthase. Whereas the parent 5-phosphonoalkyl-6-D-ribitylaminopyrimidinediones were lumazine synthase inhibitors and did not inhibit riboflavin synthase, the amide-containing derivatives inhibited riboflavin synthase and were only very weak or inactive as lumazine synthase inhibitors. Molecular modeling of inhibitor-lumazine synthase complexes did not reveal a structural basis for these unexpected findings. However, molecular modeling of one of the inhibitors with E. coli riboflavin synthase demonstrated that the active site of the enzyme could readily accommodate two ligand molecules.