diphenyl (1-amino-3-methyl)butylphosphonate | 73270-43-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: diphenyl (1-amino-3-methyl)butylphosphonate
• 英文别名: Diphenyl (1-amino-3-methylbutyl)phosphonate；1-diphenoxyphosphoryl-3-methylbutan-1-amine
• CAS: 73270-43-6
• 化学式: C₁₇H₂₂NO₃P
• 分子量: 319.34
• InChiKey: KBDLEVJSRJXEGL-UHFFFAOYSA-N

物化性质

• 熔点：
  57-58 °C
• 沸点：
  421.4±37.0 °C(Predicted)
• 密度：
  1.155±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  22
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  61.6
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  diphenyl (1-amino-3-methyl)butylphosphonate 在 potassium fluoride 、 18-冠醚-6 作用下， 以 1,4-二氧六环 为溶剂， 反应 120.0h， 生成 (2R,3R)-2,3-dibenzoyloxy-4-[[(1R)-1-dimethoxyphosphoryl-3-methylbutyl]amino]-4-oxobutanoic acid
  参考文献：
  名称：

  Kafarski, Pawel; Lejczak, Barbara; Szewczyk, Jerzy, Canadian Journal of Chemistry, 1983, vol. 61, p. 2425 - 2430

  摘要：

  DOI：
• 作为产物：
  描述：

  亚磷酸三苯酯 在 氢溴酸 、 copper(II) bis(trifluoromethanesulfonate) 、 溶剂黄146 作用下， 以 二氯甲烷 为溶剂， 反应 8.0h， 生成 diphenyl (1-amino-3-methyl)butylphosphonate
  参考文献：
  名称：

  Direct ¹⁸F-Labeling of Biomolecules via Spontaneous Site-Specific Nucleophilic Substitution by F^– on Phosphonate Prostheses

  摘要：

  DOI：

  10.1021/acs.orglett.1c01211

文献信息

• Phosphorus amino acid analogs as inhibitors of leucine aminopeptidase
  作者：Peter P. Giannousis、Paul A. Bartlett

  DOI：10.1021/jm00392a014

  日期：1987.9

  A variety of phosphorus amino acid and dipeptide analogues have been synthesized and evaluated as inhibitors of the metalloenzyme leucine aminopeptidase from porcine kidney. Two phosphonate dipeptides were found to be modest inhibitors of the enzyme (8e, Ki = 58 microM; 8h, Ki = 340 microM). The phosphinic acid (17-OH) and phosphinamide (17-NH2) analogues related to bestatin were prepared by condensation

  已经合成了多种磷氨基酸和二肽类似物，并被评价为来自猪肾脏的金属酶亮氨酸氨基肽酶的抑制剂。发现两种膦酸酯二肽是该酶的适度抑制剂（8e，Ki = 58 microM； 8h，Ki = 340 microM）。与贝斯汀相关的次膦酸（17-OH）和次膦酰胺（17-NH2）类似物是通过使次膦酸酯氨基酸衍生物11通过三价亚膦酸酯12与亮氨酸异氰酸酯衍生物13缩合而制备的。在抑制LAP方面无异常（17-O-，Ki = 56 microM； 17-NH2，Ki = 40 microM）。还评估了一系列简单的（α-氨基烷基）膦酸和-次膦酸，发现最有效的抑制剂是L-Leu和L-Phe [R] -3e的膦酸类似物，Ki = 0.23 microM; （R）-3h，Ki ＝0.42μM）。对于（R）-3e（kon = 400 +/- 55 M-1 s-1）和（R）-3h（kon = 445 +/- 50 M-1
• Remote Binding Energy in Antibody Catalysis:  Studies of a Catalytically Unoptimized Specificity Pocket
  作者：Herschel Wade、Thomas S. Scanlan

  DOI：10.1021/ja983017e

  日期：1999.2.1

  Binding interactions remote from the hydrolytic reaction center have been probed with substrate and phosphonate transition state analogues to understand how these types of interactions are used to promote catalysis in the 17E8 system, We find that the hapten-generated recogniton pocket in 17E8 has properties that are analogous to those of specificity pockets in enzymes, pie have also found that there are specific requirements to form catalytically productive interactions between the side chain and the recognition pocket including conformation, size, and geometry. An additional requirement includes Favorable simultaneous interactions between the side chain and binding packet along with favorable interactions with the oxyanion hole. The 17E8 side chain recognition pocket seems to be less catalytically efficient than analogous pockets in enzymatic systems. The apparent binding energy gained from the methylene-packet interactions in the 17E8 system is significantly smaller than those observed in natural enzymes. Furthermore, 17E8 does not use specific interactions in the recognition pocket to significantly affect catalytic turnover (k(cat)) which is thought to be a trait of an unoptimized catalyst. Analysis of the crystal structure of the 17E8,hapten complex has allowed for the identification of differences between the active sites of 17E8; and several proteases, The identified differences give insight to the sources of the inefficient use of binding energy.
• Towards the identification of unknown neuropeptide precursor-processing enzymes: Design and synthesis of a new family of dipeptidyl phosphonate activity probes for substrate-based protease identification
  作者：Eduard Sabidó、Teresa Tarragó、Ernest Giralt

  DOI：10.1016/j.bmc.2010.09.066

  日期：2010.12

  Specific proteolytic processing of inactive precursors is an exquisite cellular mechanism that triggers the activation of numerous physiologic peptides and proteins. This process ensures the generation of biologically active peptides, such as many neuropeptides and peptide hormones, in the appropriate cellular compartments at the right time, and its failure leads to several pathological conditions. Identification of the proteases involved in this limited proteolysis is, therefore, an essential step for the subsequent establishment of new therapeutic targets. As a first effort along this line, we synthesized eight new dipeptidyl phosphonate activity-based probes and used them to explore the soluble proteome from mouse brain and pituitary gland for substrate-based protease identification both by in-gel analysis and mass spectrometry. (C) 2010 Elsevier Ltd. All rights reserved.
• Diphenyl 1-Aminoalkanephosphonates
  作者：Józef Oleksyszyn、Lidia Subotkowska、Przemysław Mastalerz

  DOI：10.1055/s-1979-28903

  日期：——
• Transesterification of Diphenyl Phosphonates using the Potassium Fluoride/Crown Ether/Alcohol System; Part 2. The Use of Diphenyl 1-Aminoalkanephosphonates in Phosphonopeptide Synthesis
  作者：Barbara Lejczak、Paweł Kafarski、Jerzy Szewczyk

  DOI：10.1055/s-1982-29818

  日期：——