N-benzoyl-Gly-Phe | 4703-39-3

• 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-benzoyl-Gly-Phe
• 英文别名: N-Benzoyl-glycyl-DL-phenylalanin；N-Benzoyl-glycyl-phenylalanin；N-hippuroyl-3-phenyl-alanine；N-hippuroyl-phenylalanine；N-(N-Benzoyl-glycyl)-DL-phenylalanin；N-hippuroyl-DL-phenylalanine；N-Hippuroyl-DL-phenylalanin；N-Hippuroyl-phenylalanin；Benzoyl-glycyl-dl-phenylalanin；N-benzoylglycylphenylalanine；Hippuryl-dl-phenylalanin；N-Hippurylphenylalanine；2-[(2-benzamidoacetyl)amino]-3-phenylpropanoic acid
• CAS: 4703-39-3
• 化学式: C₁₈H₁₈N₂O₄
• 分子量: 326.352
• InChiKey: CCLJGZGVIQBNDH-UHFFFAOYSA-N

物化性质

• 熔点：
  172 °C
• 沸点：
  673.3±55.0 °C(Predicted)
• 密度：
  1.267±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  24
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.17
• 拓扑面积：
  95.5
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-benzoyl-Gly-Phe 在 盐酸 、 乙醇 、 一水合肼 作用下， 生成 N-hippuroyl-DL-phenylalanine hydrazide
  参考文献：
  名称：

  Curtius; Mueller, Journal fur praktische Chemie (Leipzig 1954), 1904, vol. <2> 70, p. 226

  摘要：

  DOI：
• 作为产物：
  描述：

  glycylphenylalanine 在 碳酸氢钠 作用下， 生成 N-benzoyl-Gly-Phe
  参考文献：
  名称：

  Abderhalden; Herrmann, Fermentforschung, vol. 10, p. 154

  摘要：

  DOI：

文献信息

• Photocatalytic decarboxylative alkenylation of α-amino and α-hydroxy acid-derived redox active esters by NaI/PPh₃ catalysis
  作者：Ya-Ting Wang、Ming-Chen Fu、Bin Zhao、Rui Shang、Yao Fu

  DOI：10.1039/c9cc09654j

  日期：——

  Herein, we report the photocatalytic decarboxylative alkenylation reactions of N-(acyloxy)phthalimide derived from α-amino and α-hydroxy acids with 1,1-diarylethene, and with cinnamic acid derivatives through double decarboxylation, using sodium iodide and triphenylphosphine as redox catalysts. The reaction proceeds under mild irradiation conditions with visible blue light (440 nm or 456 nm) in an

  在本文中，我们报道了使用碘化钠和三苯基膦作为氧化还原催化剂，由α-氨基和α-羟基酸衍生的N-（酰氧基）邻苯二甲酰亚胺与1,1-二芳基乙烯和肉桂酸衍生物通过双重脱羧的光催化脱羧烯基化反应。。该反应在丙酮溶剂中在温和的辐照条件下用可见的蓝光（440 nm或456 nm）进行，而无需使用基于过渡金属或有机染料的光氧化还原催化剂。反应通过N-（酰氧基）邻苯二甲酰亚胺和NaI / PPh 3的瞬时自组装生色团的光活化而进行。溶剂化在反应性中起关键作用。
• Photocatalytic Decarboxylative Reduction of Carboxylic Acids and Its Application in Asymmetric Synthesis
  作者：Carlo Cassani、Giulia Bergonzini、Carl-Johan Wallentin

  DOI：10.1021/ol5019294

  日期：2014.8.15

  The decarboxylative reduction of naturally abundant carboxylic acids such as α-amino acids and α-hydroxy acids has been achieved via visible-light photoredox catalysis. By using an organocatalytic photoredox system, this method offers a mild and rapid entry to a variety of high-value compounds including medicinally relevant scaffolds. Regioselective decarboxylation is achieved when differently substituted

  已经通过可见光光氧化还原催化实现了天然丰富的羧酸如α-氨基酸和α-羟基酸的脱羧还原。通过使用有机催化光氧化还原系统，此方法可轻松温和地进入包括药用相关支架在内的各种高价值化合物。当使用不同取代的二羧酸时，实现了区域选择性脱羧。从天然α-氨基酸开始，该方法在合成富含对映体的1-芳基-2,2,2-三氟乙基手性胺中的应用进一步证明了开发的光催化脱羧还原方案的实用性。
• Compositions for the delivery of antigens
  申请人：Emisphere Technologies, Inc.

  公开号：US05958457A1

  公开（公告）日：1999-09-28

  The present invention relates to compositions and methods for orally delivering antigens. The antigen and an adjuvant are combined with an acylated amino acid or polyamino acid and, a sulfonated amino acids or polyamino acid, or a salt of the foregoing.

  本发明涉及用于口服给药抗原的组合物和方法。将抗原和佐剂与酰化氨基酸或聚氨基酸以及磺化氨基酸或聚氨基酸或上述化合物的盐结合。
• Method of detecting procarboxypeptidase A and carboxypeptidase A levels in biological fluids
  申请人：——

  公开号：US20010055785A1

  公开（公告）日：2001-12-27

  Methods of enhancing sensitivity and specificity of an assay measuring enzymatic activity in a sample by measuring enzymatic activity in the sample in the presence and absence of a specific inhibitor of the enzymatic activity are provided. Methods of measuring carboxypeptidase A levels and total carboxypeptidase A levels, wherein procarboxypeptidase A is converted to carboxypeptidase A by addition of clostripain, in a biological fluid with a carboxypeptidase A substrate, specificity of which is enhanced by addition of a carboxypeptidase A specific inhibitor are also provided. In addition, methods of diagnosing acute pancreatitis by measurement of carboxypeptidase A levels and pancreatic cancer by measurement of total carboxypeptidase A levels are also provided.

  本发明提供了通过在酶活性特异性抑制剂存在和不存在的情况下测量样品中的酶活性来提高测量样品中酶活性的检测灵敏度和特异性的方法。还提供了测量生物流体中羧肽酶 A 水平和总羧肽酶 A 水平的方法，其中原羧肽酶 A 通过添加梭菌毒素转化为羧肽酶 A，生物流体中的羧肽酶 A 底物通过添加羧肽酶 A 特异性抑制剂提高了特异性。此外，还提供了通过测量羧肽酶 A 水平诊断急性胰腺炎和通过测量总羧肽酶 A 水平诊断胰腺癌的方法。
• Methods for stabilization and renaturation of proteins using nucleolar protein B23
  申请人：The University of Mississippi Medical Center

  公开号：US20020115169A1

  公开（公告）日：2002-08-22

  The present invention provides methods for stabilizing proteins, preventing protein aggregation, renaturation of previously-denatured proteins, reactivating a protein that has been inactivated by denaturation, preserving enzyme activities under conditions of elevated temperatures, inducing thermotolerance in bacteria, increasing the temperature optimum for the activity of an enzyme, and preventing formation of inclusion bodies by bacterially-expressed recombinant proteins.

  本发明提供了稳定蛋白质、防止蛋白质聚集、使先前变性的蛋白质重新变性、使因变性而失活的蛋白质重新活化、在高温条件下保持酶活性、诱导细菌的耐热性、提高酶活性的最适温度以及防止细菌表达的重组蛋白质形成包涵体的方法。