Hmb-Gly-OBzl | 1033922-34-7

• 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: Hmb-Gly-OBzl
• 英文别名: Benzyl 2-[(2-hydroxy-4-methoxyphenyl)methylamino]acetate；benzyl 2-[(2-hydroxy-4-methoxyphenyl)methylamino]acetate
• CAS: 1033922-34-7
• 化学式: C₁₇H₁₉NO₄
• 分子量: 301.342
• InChiKey: PYXKAQSDGUXNEI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  22
• 可旋转键数：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.24
• 拓扑面积：
  67.8
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  Hmb-Gly-OBzl 、 Fmoc-L-缬氨酸 在 N,N'-二异丙基碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 反应 12.0h， 以2.95 g的产率得到Fmoc-Val-HmbGly-OBzl
  参考文献：
  名称：

  Synthesis and purification of aggregation-prone hydrophobic peptides by the incorporation of an Fmoc dipeptide with the peptide bond protected with a modified 2-hydroxy-4-methoxybenzyl (Hmb) group

  摘要：

  The dipeptide Fmoc-Val-(2-hydroxy-4-methoxybenzyl)Gly-OBzl was synthesized and the 2-hydroxyl group carbamoylated to give a Boc-N(CH(3))CH(2)CH(2)N(CH(3))CO-, (Boc-Nmec-) modification of the 2-hydroxy-4-methoxybenzyl (Hmb) group. After catalytic hydrogenation and purification, the resulting dipeptide Fmoc-Val-(Boc-Nmec-Hmb)Gly-OH was used in solid phase peptide synthesis. During treatment with TFA, the peptide was released from the resin and the Boc group cleaved. The peptide could then be purified with an alkylated peptide bond carrying a cationic charge that both increased the solubility of the peptide during the purification steps and facilitated analysis by MALDI-TOF mass spectrometry. The Nmec group was cleaved by intramolecular cyclization under slightly alkaline conditions, followed by cleavage of the Hmb group by TFA to give the fully deprotected peptide. (c) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetlet.2008.04.055
• 作为产物：
  描述：

  2-羟基-4-甲氧基苯甲醛 、 甘氨酸苄酯盐酸盐 在 sodium tetrahydroborate 作用下， 以 乙醇 为溶剂， 反应 0.67h， 以62.9%的产率得到Hmb-Gly-OBzl
  参考文献：
  名称：

  Synthesis and purification of aggregation-prone hydrophobic peptides by the incorporation of an Fmoc dipeptide with the peptide bond protected with a modified 2-hydroxy-4-methoxybenzyl (Hmb) group

  摘要：

  The dipeptide Fmoc-Val-(2-hydroxy-4-methoxybenzyl)Gly-OBzl was synthesized and the 2-hydroxyl group carbamoylated to give a Boc-N(CH(3))CH(2)CH(2)N(CH(3))CO-, (Boc-Nmec-) modification of the 2-hydroxy-4-methoxybenzyl (Hmb) group. After catalytic hydrogenation and purification, the resulting dipeptide Fmoc-Val-(Boc-Nmec-Hmb)Gly-OH was used in solid phase peptide synthesis. During treatment with TFA, the peptide was released from the resin and the Boc group cleaved. The peptide could then be purified with an alkylated peptide bond carrying a cationic charge that both increased the solubility of the peptide during the purification steps and facilitated analysis by MALDI-TOF mass spectrometry. The Nmec group was cleaved by intramolecular cyclization under slightly alkaline conditions, followed by cleavage of the Hmb group by TFA to give the fully deprotected peptide. (c) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetlet.2008.04.055

文献信息

• Synthesis and purification of aggregation-prone hydrophobic peptides by the incorporation of an Fmoc dipeptide with the peptide bond protected with a modified 2-hydroxy-4-methoxybenzyl (Hmb) group
  作者：Karolina Wahlström、Ove Planstedt、Anders Undén

  DOI：10.1016/j.tetlet.2008.04.055

  日期：2008.6

  The dipeptide Fmoc-Val-(2-hydroxy-4-methoxybenzyl)Gly-OBzl was synthesized and the 2-hydroxyl group carbamoylated to give a Boc-N(CH(3))CH(2)CH(2)N(CH(3))CO-, (Boc-Nmec-) modification of the 2-hydroxy-4-methoxybenzyl (Hmb) group. After catalytic hydrogenation and purification, the resulting dipeptide Fmoc-Val-(Boc-Nmec-Hmb)Gly-OH was used in solid phase peptide synthesis. During treatment with TFA, the peptide was released from the resin and the Boc group cleaved. The peptide could then be purified with an alkylated peptide bond carrying a cationic charge that both increased the solubility of the peptide during the purification steps and facilitated analysis by MALDI-TOF mass spectrometry. The Nmec group was cleaved by intramolecular cyclization under slightly alkaline conditions, followed by cleavage of the Hmb group by TFA to give the fully deprotected peptide. (c) 2008 Elsevier Ltd. All rights reserved.