N-苄氧羰基-D-酪氨酸苄酯 | 920306-95-2

• 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
• 中文名称: N-苄氧羰基-D-酪氨酸苄酯
• 英文名称: N-benzyloxycarbonyl-D-tyrosine benzyl ester
• 英文别名: Benzyl (2R)-2-{[(benzyloxy)carbonyl]amino}-3-(4-hydroxyphenyl)propanoate；benzyl (2R)-3-(4-hydroxyphenyl)-2-(phenylmethoxycarbonylamino)propanoate
• CAS: 920306-95-2
• 化学式: C₂₄H₂₃NO₅
• 分子量: 405.45
• InChiKey: MUSDDUICYXQXRT-JOCHJYFZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.7
• 重原子数：
  30
• 可旋转键数：
  10
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  84.9
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-苄氧羰基-D-酪氨酸苄酯 在 palladium on activated charcoal 氢气 、 溶剂黄146 、 N,N'-二环己基碳二亚胺 、 copper(l) chloride 作用下， 以 水 、 乙酸乙酯 为溶剂， 反应 15.5h， 生成 4-O-(β-L-glucopyranosyl)-D-tyrosine
  参考文献：
  名称：

  Synthesis and biological activities of analogs of d-glucosyl-l-tyrosine, a humoral factor that stimulates transcription of the acyl-CoA binding protein in the pheromone gland of the Silkmoth, Bombyx mori

  摘要：

  beta-D-Glucosyl-O-L-tyrosine (1) is a Immoral factor that stimulates transcription of the acyl-CoA binding protein (ACBP) in the pheromone gland of the Silkmoth, Bombyx mori. This paper describes stereoselective synthesis of five analogs that changed the sugar and/or amino acid part in 1 and their stimulatory activities on the ACBP transcription in the pheromone gland of B. mori. Among the analogs tested, beta-D-galactosyl-O-L-tyrosine showed a 115 potency compared to the activity of 1. (c) 2006 Published by Elsevier Ltd.

  DOI：

  10.1016/j.bmc.2006.10.008
• 作为产物：
  描述：

  溴甲苯 、 N-苄氧羰基-D-酪氨酸 在 碳酸氢钠 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 21.0h， 以94%的产率得到N-苄氧羰基-D-酪氨酸苄酯
  参考文献：
  名称：

  Synthesis and biological activities of analogs of d-glucosyl-l-tyrosine, a humoral factor that stimulates transcription of the acyl-CoA binding protein in the pheromone gland of the Silkmoth, Bombyx mori

  摘要：

  beta-D-Glucosyl-O-L-tyrosine (1) is a Immoral factor that stimulates transcription of the acyl-CoA binding protein (ACBP) in the pheromone gland of the Silkmoth, Bombyx mori. This paper describes stereoselective synthesis of five analogs that changed the sugar and/or amino acid part in 1 and their stimulatory activities on the ACBP transcription in the pheromone gland of B. mori. Among the analogs tested, beta-D-galactosyl-O-L-tyrosine showed a 115 potency compared to the activity of 1. (c) 2006 Published by Elsevier Ltd.

  DOI：

  10.1016/j.bmc.2006.10.008

文献信息

• <i>N</i>,<i>N</i>′-Dialkyldiamide-Type Phosphate Protecting Groups for Fmoc Synthesis of Phosphotyrosine-Containing Peptides: Optimization of the Alkyl Group
  作者：Masaaki Ueki、Mitsutaka Goto、Jin Okumura、Yusuke Ishii

  DOI：10.1246/bcsj.71.1887

  日期：1998.8

  Synthesis and evaluation of three Fmoc–phosphotyrosine derivatives with a phosphate group protected as N,N′-dialkyldiamide (alkyl = Prn, Pri, and Bui) were studied. All the derivatives were obtained as crystals, among which the Buiderivative (4c) was the best in ease of preparation and excellence in cleavage property. Solid phase synthesis of a methionine-containing peptide, H–Tyr(PO3H2)–Val–Pro–Met–Leu–OH

  研究了三种 Fmoc-磷酸酪氨酸衍生物的合成和评估，其中磷酸基团被保护为 N,N'-二烷基二酰胺（烷基 = Prn、Pri 和 Bui）。所有衍生物均以晶体形式获得，其中以合成衍生物(4c)的制备容易性和裂解性能最好。含甲硫氨酸的肽 H-Tyr(PO3H2)-Val-Pro-Met-Leu-OH 的固相合成可以毫无问题地完成。
• Synthesis and biological activities of analogs of d-glucosyl-l-tyrosine, a humoral factor that stimulates transcription of the acyl-CoA binding protein in the pheromone gland of the Silkmoth, Bombyx mori
  作者：Shunya Takahashi、Keiko Hasumi、Atsushi Ohnishi、Hiroyuki Koshino、Shogo Matsumoto

  DOI：10.1016/j.bmc.2006.10.008

  日期：2007.1

  beta-D-Glucosyl-O-L-tyrosine (1) is a Immoral factor that stimulates transcription of the acyl-CoA binding protein (ACBP) in the pheromone gland of the Silkmoth, Bombyx mori. This paper describes stereoselective synthesis of five analogs that changed the sugar and/or amino acid part in 1 and their stimulatory activities on the ACBP transcription in the pheromone gland of B. mori. Among the analogs tested, beta-D-galactosyl-O-L-tyrosine showed a 115 potency compared to the activity of 1. (c) 2006 Published by Elsevier Ltd.