N-tert-butoxycarbonyl-D-glutamic acid α-p-nitrophenyl-γ-benzyl ester | 76379-00-5

• 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: N-tert-butoxycarbonyl-D-glutamic acid α-p-nitrophenyl-γ-benzyl ester
• 英文别名: t-butoxycarbonyl-D-glutamic acid α-p-nitrophenyl γ-benzyl diester；Boc-D-glutamic acid α-p-nitrophenyl γ-benzyl diester；Boc-Glu(OBzl)-ONp；BOC-D-Glu-α-ONp-γ-OBn；5-O-benzyl 1-O-(4-nitrophenyl) (2R)-2-[(2-methylpropan-2-yl)oxycarbonylamino]pentanedioate
• CAS: 76379-00-5
• 化学式: C₂₃H₂₆N₂O₈
• 分子量: 458.468
• InChiKey: FWDKXKMKRUDOMG-LJQANCHMSA-N

物化性质

• 沸点：
  618.0±55.0 °C(Predicted)
• 密度：
  1.258±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  33
• 可旋转键数：
  12
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  137
• 氢给体数：
  1
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  N-tert-butoxycarbonyl-D-glutamic acid α-p-nitrophenyl-γ-benzyl ester 在 钯 ammonium hydroxide 、 氢气 、 溶剂黄146 、 三氟乙酸 作用下， 以 四氢呋喃 、 甲醇 、 乙腈 为溶剂， 反应 35.58h， 生成 (R)-4-{2-[(R)-2-((3R,4R,5S,6R)-3-Acetylamino-2,5-dihydroxy-6-hydroxymethyl-tetrahydro-pyran-4-yloxy)-propionylamino]-2-methyl-propionylamino}-4-carbamoyl-butyric acid
  参考文献：
  名称：

  具有增强佐剂活性的胞壁酰二肽类似物的合成

  摘要：

  N-Acetylmuramyl-L-alanyl-D-isoglutamine (MDP) 和十三个新的类似物是通过常规有机化学方法合成的，使用二环己基碳二亚胺-N-羟基-5-降冰片烯-2,3-二甲酰亚胺作为偶联剂。测定了它们在豚鼠中诱导对 N-乙酰基-3-(4-arsonophenylazo)-L-酪氨酸的迟发型超敏反应的能力。结果表明，与 MDP 中乳酸部分相邻的 α-氨基酸的存在对于高生物活性很重要，缬氨酸类似物具有最有利的作用。讨论了构效关系。

  DOI：

  10.1246/bcsj.53.2570
• 作为产物：
  描述：

  D-谷氨酸-5-苄酯 在 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 水 、 乙酸乙酯 、 N,N-二甲基甲酰胺 为溶剂， 反应 2.0h， 生成 N-tert-butoxycarbonyl-D-glutamic acid α-p-nitrophenyl-γ-benzyl ester
  参考文献：
  名称：

  具有增强佐剂活性的胞壁酰二肽类似物的合成

  摘要：

  N-Acetylmuramyl-L-alanyl-D-isoglutamine (MDP) 和十三个新的类似物是通过常规有机化学方法合成的，使用二环己基碳二亚胺-N-羟基-5-降冰片烯-2,3-二甲酰亚胺作为偶联剂。测定了它们在豚鼠中诱导对 N-乙酰基-3-(4-arsonophenylazo)-L-酪氨酸的迟发型超敏反应的能力。结果表明，与 MDP 中乳酸部分相邻的 α-氨基酸的存在对于高生物活性很重要，缬氨酸类似物具有最有利的作用。讨论了构效关系。

  DOI：

  10.1246/bcsj.53.2570

文献信息

• Synthesis and binding affinities of cyclic and related linear analogs of CCK8 selective for central receptors
  作者：Bruno Charpentier、Adeline Dor、Pierre Roy、Patrick England、Pham Hung、Christiane Durieux、Bernard P. Roques

  DOI：10.1021/jm00126a007

  日期：1989.6

  To investigate the role of the sulfate group and the influence of cyclization on the biological properties of conformationally constrained CCK8 analogues, three series of compounds were synthesized: Boc-Glu-Tyr-Nle-D-Lys-Trp-Nle-Asp-Phe-NH2 (1), Boc-Glu-Tyr(SO3H)-Nle-D-Lys-Trp-Nle-Asp-Phe-NH2 (2), and Boc-Glu-Tyr-(SO3H)-Nle-D-Lys-Trp-Nle-Asp-Phe-NH2 (3) (series A); Boc-D-Glu-Tyr-Nle-D-Lys-Trp-Nle-Asp-Phe-NH2 (4), Boc-D-Glu-Tyr(SO3H)-Nle-D-Lys-Trp-Nle-Asp-Phe-NH2 (5), Boc-D-Glu-Tyr(SO3H)-Nle-D-Lys-Trp-Nle-Asp-Phe-NH2 (6), and Boc-D-Glu-Tyr(SO3H)-Nle-D-Nle-Trp-Asp-Phe-NH2 (7) (series B); and Boc-gamma-D-Glu-Tyr-Nle-D-Lys-Trp-Nle-Asp-Phe-NH2 (8), Boc-gamma-D-Glu-Tyr(SO3H)-Nle-D-Lys-Trp-Nle-Asp-Phe-NH2 (9), and Boc-gamma-D-Glu-Tyr-(SO3H)-Nle-D-Lys-Trp-Nle-Asp-Phe-NH2 (10) (series C). The selectivity of these peptides was studied by measuring their ability to displace [3H]propionyl-CCK8 from guinea pig brain and pancreatic membranes. All the peptides displayed low affinities (KI values around 10(-6) M) for the pancreatic receptors (A type). In contrast, both sulfated and nonsulfated cyclic analogues displayed high affinities for central-type binding sites (B type), especially compounds belonging to series C [KI(8) = 4.7 nM and KI(9) = 0.56 nM]. In all series the linear analogues had relatively poor affinities (KI approximately 300 nM) for B-type receptors. Compound 9 was the most potent (KI = 0.56 nM) and selective [KI(pancreas)/KI(brain) = 4464] for central-type CCK receptors of guinea pig. The cyclization of the N-terminal region of CCK8 permits one therefore to obtain probes for central receptors, and small changes directed toward the cyclic part modulate the affinity for these receptors.
• Activation for Catalysis of Penicillin-Binding Protein 2a from Methicillin-Resistant <i>Staphylococcus </i><i>a</i><i>ureus</i> by Bacterial Cell Wall
  作者：Cosimo Fuda、Dusan Hesek、Mijoon Lee、Ken-ichiro Morio、Thomas Nowak、Shahriar Mobashery

  DOI：10.1021/ja0434376

  日期：2005.2.1

  Methicillin-resistant Staphylococcus aureus (MRSA) has acquired a unique penicillin-binding protein (PBP), PBP 2a, which has rendered the organism resistant to the action of all available beta-lactam antibiotics. The X-ray structure of PBP 2a shows the active site in a closed conformation, consistent with resistance to inhibition by beta-lactam antibiotics. However, it is known that PBP 2a avidly cross-links the S. aureus cell wall, which is its physiological function. It is shown herein that synthetic fragments of the bacterial cell wall bind in a saturable manner to PBP 2a and cause a conformational change in the protein that makes the active site more accessible to binding to a beta-lactam antibiotic. These observations and measurements point to a novel strategy by nature to keep the active site of PBP 2a sheltered from the inhibitory activity of the antibiotics, yet it becomes available to the polymeric cell wall by a requisite conformational change for the critical cell wall cross-linking reaction.
• Synthesis of lipophilic ?-alkylamides of N-acetylmuramoyl-L-alanyl-D-glutamic acid
  作者：A. E. Zemlyakov、V. V. Terekhov、V. Ya. Chirva

  DOI：10.1007/bf00607544

  日期：——
• CHARPENTIER, B.;DOR, A.;ROY, P.;ENGLAND, P.;PHAM, H.;DURIEUX, C., J. MED. CHEM., 32,(1989) N, C. 1184-1190
  作者：CHARPENTIER, B.、DOR, A.、ROY, P.、ENGLAND, P.、PHAM, H.、DURIEUX, C.

  DOI：——

  日期：——
• ZEMLYAKOV, A. E.;TEREXOV, V. V.;CHIRVA, V. YA., XIMIYA PRIROD. SOED.,(1990) N, S. 249-252
  作者：ZEMLYAKOV, A. E.、TEREXOV, V. V.、CHIRVA, V. YA.

  DOI：——

  日期：——