(2R)-2-methyl-5-(tert-butoxycarbonylamino)valeric acid | 1352407-82-9

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: (2R)-2-methyl-5-(tert-butoxycarbonylamino)valeric acid
• 英文别名: Boc-(R)-5-amino-2-methylpentanoic acid；(R)-5-((tert-Butoxycarbonyl)amino)-2-methylpentanoic acid；(2R)-2-methyl-5-[(2-methylpropan-2-yl)oxycarbonylamino]pentanoic acid
• CAS: 1352407-82-9
• 化学式: C₁₁H₂₁NO₄
• 分子量: 231.292
• InChiKey: OBZVEXKLKXLILY-MRVPVSSYSA-N

物化性质

• 沸点：
  374.0±25.0 °C(Predicted)
• 密度：
  1.063±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  16
• 可旋转键数：
  7
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.82
• 拓扑面积：
  75.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  在 palladium 10% on activated carbon 、 水 、 氢气 、 双氧水 、 碳酸氢钠 、 lithium hydroxide 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 甲醇 、 水 、 溶剂黄146 为溶剂， 反应 32.33h， 生成 (2R)-2-methyl-5-(tert-butoxycarbonylamino)valeric acid
  参考文献：
  名称：

  Modulation of the Passive Permeability of Semipeptidic Macrocycles: N- and C-Methylations Fine-Tune Conformation and Properties

  摘要：

  DOI：

  10.1021/acs.jmedchem.0c02036

文献信息

• [EN] DIRECTED CONJUGATION TECHNOLOGIES<br/>[FR] TECHNOLOGIES DE CONJUGAISON DIRIGÉE
  申请人：KLEO PHARMACEUTICALS INC

  公开号：WO2021102052A1

  公开（公告）日：2021-05-27

  Among other things, the present disclosure provides technologies for site-directed conjugation of various moieties of interest to target agents. In some embodiments, the present disclosure utilizes target binding moieties to provide high conjugation efficiency and selectivity. In some embodiments, provided technologies are useful for preparing antibody conjugates.

  本公开提供了用于将各种感兴趣的分子与目标剂进行定点偶联的技术。在某些实施方式中，本公开利用目标结合分子以提供高偶联效率和选择性。在某些实施方式中，所提供的技术可用于制备抗体偶联物。
• Conformationally restricted analogs of the direct thrombin inhibitor FM 19
  作者：Elizabeth A. Girnys、Vanessa R. Porter、Henry I. Mosberg

  DOI：10.1016/j.bmc.2011.10.045

  日期：2011.12

  The serine protease thrombin plays several key roles in the clotting cascade within the hemostatic system, such as in fibrin formation and platelet activation. Thus, development of an inhibitor that binds to the enzyme's active site (a direct thrombin inhibitor) offers an approach for the treatment of thrombus-associated diseases. Previous structure-activity relationship studies originally based on the bradykinin breakdown product Arg-Pro-Pro-Gly-Phe (RPPGF) led to the development of lead compound FM 19 (D-Arg-Oic-Pro-D-Ala-Phe(p-Me)-NH2). The recently determined X-ray structure of FM 19 in the active site of thrombin has revealed sites of modification to potentially improve inhibition. In this study, we report the synthesis and biological characterization of nine peptides that replace only the D-Arg residue of the FM 19 sequence, investigating ways to add conformational restriction, modification of the basic moiety at the end of the side chain, and removal of the charge from the N-terminus. Two of these peptides, 6 and 7 (IC50 values of 0.51 and 0.45 mu M, respectively), show similar potency to the best compounds in the FM 19 series reported thus far. (C) 2011 Elsevier Ltd. All rights reserved.