HCl*HGly-pNA | 54643-65-1

• 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: HCl*HGly-pNA
• 英文别名: H-Gly-PNA.HCl；2-amino-N-(4-nitrophenyl)acetamide;hydrochloride
• CAS: 54643-65-1
• 化学式: C₈H₉N₃O₃*ClH
• 分子量: 231.639
• InChiKey: IZBAOLMLWUOHIP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.91
• 重原子数：
  15
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  101
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  Z-L-苯丙氨酸苄酯 、 HCl*HGly-pNA 在 subtilisin BPN' 、 三乙胺 作用下， 以 水 、 N,N-二甲基甲酰胺 为溶剂， 以64%的产率得到Z-Phe-Gly-pNA
  参考文献：
  名称：

  Exploitation of Subtilisin BPN‘ as Catalyst for the Synthesis of Peptides Containing Noncoded Amino Acids, Peptide Mimetics and Peptide Conjugates

  摘要：

  The ability of the serine protease subtilisin BPN' to catalyze peptide bond formation between fragments containing noncoded amino acids, peptide mimetics, and peptide conjugates in a kinetic approach was explored. It was found that the enzyme accepts numerous of these types of compounds both as acyl donor and acyl acceptor. The results together with specificity studies reported by others provide an active site model as a guideline in the design of enzymatic synthesis of biologically important compounds.

  DOI：

  10.1021/ja964399w

文献信息

• Solution Synthesis of Peptide Cell Growth Stimulators
  申请人：Epstein David

  公开号：US20070213505A1

  公开（公告）日：2007-09-13

  A solution phase synthetic method for preparing basic tripeptides of the formula Gly-Xaa-Gly-X which have in various biological properties such as stimulating protein production when used as additives in a bioreactor. The basic tripeptides of the invention may be produced on gram or kilogram scale.

  一种溶液相合成方法，用于制备具有不同生物学性质的基本三肽，其化学式为Gly-Xaa-Gly-X。当作为生物反应器添加剂时，这些基本三肽可以刺激蛋白质的生产。本发明的基本三肽可以以克或千克为单位进行生产。
• Exploitation of Subtilisin BPN‘ as Catalyst for the Synthesis of Peptides Containing Noncoded Amino Acids, Peptide Mimetics and Peptide Conjugates
  作者：Wilna J. Moree、Pamela Sears、Katsuhiro Kawashiro、Krista Witte、Chi-Huey Wong

  DOI：10.1021/ja964399w

  日期：1997.4.1

  The ability of the serine protease subtilisin BPN' to catalyze peptide bond formation between fragments containing noncoded amino acids, peptide mimetics, and peptide conjugates in a kinetic approach was explored. It was found that the enzyme accepts numerous of these types of compounds both as acyl donor and acyl acceptor. The results together with specificity studies reported by others provide an active site model as a guideline in the design of enzymatic synthesis of biologically important compounds.