Boc-Asn-Tyr-OMe | 112952-80-4

• 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: Boc-Asn-Tyr-OMe
• CAS: 112952-80-4
• 化学式: C₁₉H₂₇N₃O₇
• 分子量: 409.439
• InChiKey: HBMCWSDMIMITBR-KBPBESRZSA-N

物化性质

• 沸点：
  697.8±55.0 °C(Predicted)
• 密度：
  1.257±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.36
• 重原子数：
  29.0
• 可旋转键数：
  8.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  157.05
• 氢给体数：
  4.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  Boc-Asn-Tyr-OMe 在 盐酸 、 sodium tetrahydroborate 、 三甲基氰硅烷 、 potassium tert-butylate 、 三氧化硫吡啶 、 三乙胺 、 calcium chloride 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 乙醇 、 二甲基亚砜 、 N,N-二甲基甲酰胺 为溶剂， 生成 C₂₇H₂₇N₃O₆
  参考文献：
  名称：

  Synthesis and activity of conformationally-constrained macrocyclic norstatine-based inhibitors of HIV protease

  摘要：

  Two diastereomers of a macrocyclic hydroxyamide (norstatine-based) peptide, having an 18-membered ring system, have been synthesized as HIV protease inhibitors. The (R)-diastereomer (IC50 19 nM) was similar to 17-fold weaker than an acyclic analog, but had comparable or better antiviral activity, suggesting improved cell penetration properties and/or resistance to cellular enzymes for the macrocyclic inhibitor.

  DOI：

  10.1016/0960-894x(96)00034-0
• 作为产物：
  描述：

  BOC-L-天冬酰胺 、 L-酪氨酸甲酯 在 三甲基氰硅烷 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 生成 Boc-Asn-Tyr-OMe
  参考文献：
  名称：

  Synthesis and activity of conformationally-constrained macrocyclic norstatine-based inhibitors of HIV protease

  摘要：

  Two diastereomers of a macrocyclic hydroxyamide (norstatine-based) peptide, having an 18-membered ring system, have been synthesized as HIV protease inhibitors. The (R)-diastereomer (IC50 19 nM) was similar to 17-fold weaker than an acyclic analog, but had comparable or better antiviral activity, suggesting improved cell penetration properties and/or resistance to cellular enzymes for the macrocyclic inhibitor.

  DOI：

  10.1016/0960-894x(96)00034-0

文献信息

• Amino acids and peptides. XVII. Synthesis of a tridecapeptide corresponding to the sequence 165-177 of T-kininogen (tryptic peptide) containing Gln-Val-Val-Ala-Gly sequence and the relationship between structure and effect on thiol proteinase.
  作者：NAOKI TENO、SATOSHI TSUBOI、YOSHIO OKADA、NORIO ITOH、HIROSHI OKAMOTO

  DOI：10.1248/cpb.35.3853

  日期：——

  The tridecapeptide corresponding to the sequence 165-177 of T-kininogen (tryptic peptide) (I) containing Gln-Val-Val-Ala-Gly sequence was synthesized by a conventional solution method and its effect on thiol proteinase was examined. Although Z-Gln-Val-Val-Ala-Gly-OMe showed inhibitory activity towards papain and protective activity against T-kininogen-induced inhibition of papain, the tryptic peptide obtained did not exhibit any effect on thiol proteinase. In order to study the relationship between structure and effect on thiol proteinase, several compounds (II-VI) modified with various groups at the N-terminus of the Gln-Val-Val-Ala-Gly sequence were synthesized. Peptides V and VI, which have an aromatic ring at the N-terminus, exhibited weak inhibitory and significant protective activities. A small peptide such as Gln-Val-Val-Ala-Gly might be better able to approach papain than the tryptic peptide (I), and the aromatic ring associated with Gln-Val-Val-Ala-Gly at the N-terminus apparently strengthened the binding ability of the peptide to papain.

  与T-激肽原（胰蛋白酶肽）序列165-177对应的三肽（I），含有Gln-Val-Val-Ala-Gly序列，通过传统溶液法合成，并对其对巯基蛋白酶的作用进行了研究。尽管Z-Gln-Val-Val-Ala-Gly-OMe对木瓜蛋白酶表现出抑制活性，并能保护木瓜蛋白酶免受T-激肽原诱导的抑制，但所获得的胰蛋白酶肽对巯基蛋白酶没有任何作用。为了研究结构与对巯基蛋白酶作用之间的关系，合成了几种在Gln-Val-Val-Ala-Gly序列的N-末端修改了不同基团的化合物（II-VI）。具有芳香环的肽V和VI表现出弱抑制和显著保护活性。像Gln-Val-Val-Ala-Gly这样的小肽可能比肽（I）更容易接近木瓜蛋白酶，而Gln-Val-Val-Ala-Gly N-末端的芳香环显然增强了肽与木瓜蛋白酶的结合能力。
• Immobilized<i>Aspergillus Oryzae</i>Protease Catalyzed Formation of Peptide Bonds in Organic Solvent
  作者：Ing-Lung Shih、Yun-Yin Lin、Hui-Yao Huang、Dar-Fu Tai、Kuan-Chu Chen

  DOI：10.1002/jccs.199700049

  日期：1997.6

  AbstractImmobilized Aspergillus oryzae protease (AOP) catalyzed the formation of peptide bonds between TV‐protected amino acids and amino acid esters or amides in ethyl acetate. The influences of pH and reaction time on the coupling of Boc‐L‐Tyr and Gly‐NH2 were studied. The optimal reaction condition for this enzyme catalyzed synthesis of Boc‐L‐Phe‐Gly‐NH2 (98.66%) was at pH 5.5 and a duration of 48 hours.