3-(phenylamino)phenoxyacetic acid | 305129-54-8

• 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: 3-(phenylamino)phenoxyacetic acid
• 英文别名: (3-anilino-phenoxy)-acetic acid；(3-Anilino-phenoxy)-essigsaeure
• CAS: 305129-54-8
• 化学式: C₁₄H₁₃NO₃
• 分子量: 243.262
• InChiKey: IPMDVASVXVSTHC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.89
• 重原子数：
  18.0
• 可旋转键数：
  5.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.07
• 拓扑面积：
  58.56
• 氢给体数：
  2.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  3-(phenylamino)phenoxyacetic acid 、 乙酸酐 生成 [3-(N-acetyl-anilino)-phenoxy]-acetic acid
  参考文献：
  名称：

  Ettel et al., Collection of Czechoslovak Chemical Communications, 1950, vol. 15, p. 1050,1064

  摘要：

  DOI：
• 作为产物：
  描述：

  (3-anilino-phenoxy)-acetic acid methyl ester 在 sodium hydroxide 作用下， 以 甲醇 为溶剂， 反应 1.0h， 生成 3-(phenylamino)phenoxyacetic acid
  参考文献：
  名称：

  口服有效的三肽基含羟甲基羰基异戊二烯的HIV蛋白酶抑制剂的构效关系。

  摘要：

  我们设计并合成了一种新型的拟肽类人免疫缺陷病毒蛋白酶抑制剂，其中含有独特的非天然氨基酸，别苯去甲他汀[Apns; （2S，3S）-3-氨基-2-羟基-4-苯基丁酸]，其中羟甲基羰基等排物为活性部分。通过对HIV-1蛋白酶抑制作用，对其他天冬氨酰蛋白酶的酶选择性，大鼠的抗病毒活性和药代动力学的结构-活性关系研究，发现24c（KNI-227）和24d（KNI-272，我们的第一个临床候选药物）是选择性和口服有效的HIV蛋白酶抑制剂。此外，KNI-272药代动力学特征的改善提供了两种持久且具有高生物利用度的化合物（24g：JE-2178，24h：JE-2179）。

  DOI：

  10.1248/cpb.48.1310

文献信息

• Identification of Highly Potent Human Immunodeficiency Virus Type-1 Protease Inhibitors against Lopinavir and Darunavir Resistant Viruses from Allophenylnorstatine-Based Peptidomimetics with P2 Tetrahydrofuranylglycine
  作者：Koushi Hidaka、Tooru Kimura、Rajesh Sankaranarayanan、Jun Wang、Keith F. McDaniel、Dale J. Kempf、Masanori Kameoka、Motoyasu Adachi、Ryota Kuroki、Jeffrey-Tri Nguyen、Yoshio Hayashi、Yoshiaki Kiso

  DOI：10.1021/acs.jmedchem.7b01709

  日期：2018.6.28

  The emergence of drug-resistant HIV from a widespread antiviral chemotherapy targeting HIV protease in the past decades is unavoidable and provides a challenge to develop alternative inhibitors. We synthesized a series of allophenylnorstatine-based peptidomimetics with various P-3, P-2, and P-2' moieties. The derivatives with P-2 tetrahydrofur-anylglycine (Thfg) were found to be potent against wild type HIV-1 protease and the virus, leading to a highly potent compound 21f (KNI-1657) against lopinavir/ritonavir- or darunavir-resistant strains. Co-crystal structures of 21f and the wild-type protease revealed numerous key hydrogen bonding interactions with Thfg. These results suggest that the strategy to design allophenylnorstatine-based peptidomimetics combined with Thfg residue would be promising for generating candidates to overcome multidrug resistance.
• Additional interaction of allophenylnorstatine-containing tripeptidomimetics with malarial aspartic protease plasmepsin II
  作者：Koushi Hidaka、Tooru Kimura、Yumi Tsuchiya、Mami Kamiya、Adam J. Ruben、Ernesto Freire、Yoshio Hayashi、Yoshiaki Kiso

  DOI：10.1016/j.bmcl.2007.03.052

  日期：2007.6

  Based on a highly potent allophenylnorstatine-containing inhibitor, KNI-10006, against the plasmepsins of Plasmodium falciparum, we synthesized a series of tripeptide-type compounds with various N-terminal moieties and evaluated their inhibitory activities against plasmepsin II. Certain phenylacetyl derivatives exhibited extremely high affinity with Ki values of less than 0.1 nM suggesting successful hydrophobic interactions. (C) 2007 Elsevier Ltd. All rights reserved.