α-t-butoxycarbonylamino-p-aminophenylacetic acid | 54895-25-9

• 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: α-t-butoxycarbonylamino-p-aminophenylacetic acid
• 英文别名: alpha-t-Butoxycarbonylamino-p-aminophenylacetic acid；2-(4-aminophenyl)-2-[(2-methylpropan-2-yl)oxycarbonylamino]acetic acid
• CAS: 54895-25-9
• 化学式: C₁₃H₁₈N₂O₄
• 分子量: 266.297
• InChiKey: HAKACKSZUHLWQM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  19
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  102
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  α-t-butoxycarbonylamino-p-aminophenylacetic acid 在 钯 盐酸 、 甲酸 、 氢气 、 苯甲醚 作用下， 以 1,4-二氧六环 、 甲醇 为溶剂， 反应 44.0h， 生成 β-naphthylamide of p-guanidino-DL-phenylglycine hydrochloride
  参考文献：
  名称：

  .BETA.-Naphthylamides of guanidinophenyl amino acids as substrates of aminopeptidases.

  摘要：

  合成了对-胍基-L-苯丙氨酸（GPA）和对-胍基-DL-苯甘氨酸（GPG）的β-萘甲酰胺，并将其作为牛白细胞氨肽酶（BL-APase）和猪肝氨肽酶 B（PL-APaseB）的底物与 L-精氨酸β-萘甲酰胺（Arg-βNA）进行了比较试验。BL-APase 催化 GPA-βNA 的水解速度与 Arg-βNA 一样快，而 GPG-βNA 的水解速度要慢得多。BL-AP 酶水解 GPA-βNA 的特异性常数（Vmax/Km）略大于水解 Arg-βNA。根据两种 β-萘甲酰胺底物 Km 值的比较，GPA-βNA 侧链中的苯环被认为有助于该底物与该酶特异性侧的结合。在底物浓度高于约 0.1 mM 的范围内，观察到 BL-APase 在水解 GPA-βNA 时存在底物抑制作用。PL-APaseB 不水解 GPA-βNA 也不水解 GPG-βNA，而且它们抑制该酶水解 Arg-βNA。预计 GPA-βNA 将成为研究氨基肽酶结合和催化特异性的有用底物。

  DOI：

  10.1248/cpb.36.1205
• 作为产物：
  描述：

  2-(叔丁氧羰基氧亚氨基)-2-苯乙腈 生成 α-t-butoxycarbonylamino-p-aminophenylacetic acid
  参考文献：
  名称：

  .BETA.-Naphthylamides of guanidinophenyl amino acids as substrates of aminopeptidases.

  摘要：

  合成了对-胍基-L-苯丙氨酸（GPA）和对-胍基-DL-苯甘氨酸（GPG）的β-萘甲酰胺，并将其作为牛白细胞氨肽酶（BL-APase）和猪肝氨肽酶 B（PL-APaseB）的底物与 L-精氨酸β-萘甲酰胺（Arg-βNA）进行了比较试验。BL-APase 催化 GPA-βNA 的水解速度与 Arg-βNA 一样快，而 GPG-βNA 的水解速度要慢得多。BL-AP 酶水解 GPA-βNA 的特异性常数（Vmax/Km）略大于水解 Arg-βNA。根据两种 β-萘甲酰胺底物 Km 值的比较，GPA-βNA 侧链中的苯环被认为有助于该底物与该酶特异性侧的结合。在底物浓度高于约 0.1 mM 的范围内，观察到 BL-APase 在水解 GPA-βNA 时存在底物抑制作用。PL-APaseB 不水解 GPA-βNA 也不水解 GPG-βNA，而且它们抑制该酶水解 Arg-βNA。预计 GPA-βNA 将成为研究氨基肽酶结合和催化特异性的有用底物。

  DOI：

  10.1248/cpb.36.1205

文献信息

• Substituted hydantoins
  申请人：Chen Shaoqing

  公开号：US20070197617A1

  公开（公告）日：2007-08-23

  The present invention relates to compounds of the formula methods for the preparation thereof, and methods for their use. The compounds are useful in treating diseases characterized by the hyperactivity of MEK. Accordingly the compounds are useful in the treatment of diseases, such as cancer, cognitive and CNS disorders, and inflammatory/autoimmune diseases.

  本发明涉及公式化合物的方法，其制备方法以及它们的使用方法。这些化合物在治疗由MEK高活性特征的疾病中很有用。因此，这些化合物在治疗癌症、认知和中枢神经系统疾病以及炎症/自身免疫疾病等疾病中很有用。
• METHOD FOR INHIBITING PROLIFERATION OF TUMOR CELLS
  申请人：Niu Huifeng

  公开号：US20080207563A1

  公开（公告）日：2008-08-28

  Disclosed are methods for synergistically inhibiting the proliferation of tumor cells by contacting the tumor cells with a MEK inhibitor compound and erlotinib, either sequentially or simultaneously. Also disclosed are methods for inhibiting the proliferation of tumor cells in a human, by administering to the human, sequentially or simultaneously, an amount of erlotinib and a MEK inhibitor compound, wherein the amounts are effective, in combination, to synergistically inhibit the proliferation of the tumor cells in the human.

  本文揭示了通过将肿瘤细胞与MEK抑制剂化合物和厄洛替尼接触，无论是顺序地还是同时地，协同抑制肿瘤细胞增殖的方法。还揭示了通过向人体逐步或同时施用厄洛替尼和MEK抑制剂化合物的方法，其中这些量在组合时对于协同抑制人体内肿瘤细胞增殖是有效的。
• .alpha.-amino-.alpha.-(ureidophenyl)acetamidocephalosporins
  申请人：SmithKline Corporation

  公开号：US04007173A1

  公开（公告）日：1977-02-08

  Cephalosporins with a .alpha.-amino-(ureidophenyl)acetamido substituent at position 7 are prepared by acylation of a 7-aminocephalosporin with a derivative of .alpha.-amino-p(or m)-ureidophenylacetic acid. These compounds are antibacterial agents.

  在位置7处带有α-氨基-(尿苷酰基苯基)乙酰胺取代基的头孢菌素是通过用α-氨基-p（或m）-尿苷酸苯乙酸衍生物对7-氨基头孢菌素进行酰基化制备的。这些化合物是抗菌药物。
• DIAMINOPTERIDINE DERIVATIVES
  申请人：Coish Philip D.G.

  公开号：US20120283219A1

  公开（公告）日：2012-11-08

  The present invention relates novel diaminopteridine derivatives, their compositions and method of treatment comprising the same for use as anti-infectives.

  本发明涉及一种新的二氨基喜树碱衍生物、它们的组成物和治疗方法，其中包括它们作为抗感染剂的用途。
• Asymmetric Synthesis of Conformationally Restricted <scp>l</scp>-Arginine Analogues as Active Site Probes of Nitric Oxide Synthase
  作者：Robert N. Atkinson、Lisa Moore、Joseph Tobin、S. Bruce King

  DOI：10.1021/jo982161f

  日期：1999.5.1

  Using the catalytic asymmetric Sharpless carbamate aminohydroxylation, conformationally restricted L-arginine and L-homoarginine derivatives (5-8) were prepared in good enantiomeric excess to investigate the binding requirements of L-arginine-based compounds with nitric oxide synthase. The L-arginine derivatives (5 and 6) inhibited both the inducible and neuronal isoforms of nitric oxide synthase with little isoform selectivity (5, IC50 = 42 and 144 mu M, 6, 8 and 12 mu M, respectively). The guanidine-containing compound (5) did not act as a nitric oxide producing substrate for nitric oxide synthase. The ability of these compounds to interact with the enzyme supports the idea that L-arginine-based inhibitors bind to the enzyme in a folded conformation. The L-homoarginine derivatives (7 and 8) did not interact with the enzyme as either substrates or inhibitors. The two-carbon L-arginine homologue (9), prepared from L-phenylalanine, demonstrated the greatest isoform selective inhibition of the compounds examined (IC50(iNOS) = 19 and IC50- (nNOS) = 147 mu M, IC50(nNOS)/IC(50)i(NOS) = 7.7). These results suggest isoform selective inhibition may be related to the folded conformations required for binding of these higher L-arginine homologues.