O^α-(N-Fmoc-(S)-phenylalanyl)glycolic acid | 1410925-58-4

• 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: O^α-(N-Fmoc-(S)-phenylalanyl)glycolic acid
• CAS: 1410925-58-4
• 化学式: C₂₆H₂₃NO₆
• 分子量: 445.472
• InChiKey: RYIMXXBCOSJALP-QHCPKHFHSA-N

物化性质

• 沸点：
  696.8±55.0 °C(Predicted)
• 密度：
  1.310±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.76
• 重原子数：
  33.0
• 可旋转键数：
  8.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.19
• 拓扑面积：
  101.93
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为产物：
  描述：

  tert-butyl O^α-(N-Fmoc-(S)-phenylalanyl)glycolate 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 生成 O^α-(N-Fmoc-(S)-phenylalanyl)glycolic acid
  参考文献：
  名称：

  Prohormone-substrate peptide sequence recognition by peptidylglycine α-amidating monooxygenase and its reflection in increased glycolate inhibitor potency

  摘要：

  The interactions of nineteen peptide substrates and fifteen analogous peptidomimetic glycolate inhibitors with human peptidylglycine alpha-amidating monooxygenase (PAM) have been investigated. The substrates and inhibitors are the prohormones of calcitonin and oxytocin and their analogues. PAM both secreted into the medium by and extracted from DMS53 small lung carcinoma cells has been studied. The results show that recognition of the prooxytocin and procalcitonin peptide sequences by the enzyme extends more than four and five amino acid residues, respectively, from their C-termini. This substrate sequence recognition is mirrored by increased inhibitor potency with increased peptide length in the glycolate peptidomimetics. Substitution of the C-terminal penultimate glycine and proline residues of prooxytocin and procalcitonin and their analogues with phenylalanine increases the enzyme binding affinity. However, this changes the binding mode from one that depends on peptide sequence recognition to another primarily determined by the phenylalanine moiety, for both the substrates and analogous glycolate inhibitors. Crown Copyright (C) 2012 Published by Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2012.10.004

文献信息

• Improved solid phase synthesis of peptide carboxyamidomethyl (Cam) esters for enzymatic segment condensation
  作者：Timo Nuijens、Ana Toplak、Mathijs B.A.C. van de Meulenreek、Marcel Schmidt、Michel Goldbach、Peter J.L.M. Quaedflieg

  DOI：10.1016/j.tetlet.2016.06.132

  日期：2016.8

  based on the coupling of hydroxyl protected glycolic acid to a solid support, followed by ester synthesis using an N-protected amino acid and dicyclohexyl carbodiimide with catalytic 4-dimethylaminopyridine. The second type is based on the synthesis of amino acid carboxymethyl ester building blocks, which are coupled to the solid support using standard coupling reagents and procedures. The latter procedure

  肽C末端羧酰胺甲基（Cam-）酯是酶段缩合的关键组成部分，其收率和纯度对于该策略的整体效率至关重要。尽管已经公开了一些制备它们的方法，但是肽C-末端Cam-酯的固相合成并不简单。在这里，我们描述了两种新颖的方法类型，它们以高收率和良好的纯度进行合成。第一类是基于羟基保护的乙醇酸与固体载体的偶联，然后使用N保护的氨基酸和二环己基碳二亚胺与催化的4-二甲基氨基吡啶进行酯合成。第二种是基于氨基酸羧甲基酯结构单元的合成，其使用标准偶联剂和方法偶联至固体支持物。