N-tert-butoxycarbonyl-L-methionine hydrazide | 49759-74-2

• 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: N-tert-butoxycarbonyl-L-methionine hydrazide
• 英文别名: N-tert-Butoxycarbonyl-L-methionin-hydrazid；tert-butyl [(1S)-1-(hydrazinocarbonyl)-3-(methylthio)propyl]carbamate；tert-butyl N-[(2S)-1-hydrazinyl-4-methylsulfanyl-1-oxobutan-2-yl]carbamate
• CAS: 49759-74-2
• 化学式: C₁₀H₂₁N₃O₃S
• mdl: MFCD11108874
• 分子量: 263.361
• InChiKey: NMZANECBVWWSFH-ZETCQYMHSA-N

物化性质

• 熔点：
  74 °C
• 沸点：
  475.9±40.0 °C(Predicted)
• 密度：
  1.145±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.6
• 重原子数：
  17
• 可旋转键数：
  7
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  119
• 氢给体数：
  3
• 氢受体数：
  5

安全信息

• 危险等级：
  IRRITANT

反应信息

• 作为反应物：
  描述：

  N-tert-butoxycarbonyl-L-methionine hydrazide 在 盐酸 、 sodium nitrite 作用下， 生成 N-L-methionyl-L-glutamic acid-5-benzyl ester
  参考文献：
  名称：

  Synth�se du N-ac�tyl-L-s�ryl-L-tyrosyl-L-s�ryl-L-m�thionyl-?-L-glutamate de benzyle et de peptides apparent�s

  摘要：

  AbstractN‐CBO‐L‐Seryl‐L‐tyrosyl‐L‐serine methyl ester and L‐methionyl‐γ‐benzyl‐L‐glutamate are prepared by different methods. Condensation by the hydrazideazide procedure affords N‐CBO‐L‐seryl‐L‐tyrosyl‐L‐seryl‐L‐methionyl‐γ‐benzyl‐L‐glutamate, which is shown to be optically pure by leucine‐aminopeptidase digestion. Transformation of the above N‐CBO‐tripeptide ester to the N‐acetyltripeptide ester and condensation by the hydrazide‐azide procedure with the above dipeptide gives N‐acetyl‐L‐seryl‐L‐tyrosyl‐L‐seryl‐L‐methionyl‐γ‐benzyl‐L‐glutamate. The effects produced in the course of fissure of CBO‐ and benzyl‐groups from peptides containing serine and methionine residues, using HBr and acetic acid, are studied.

  DOI：

  10.1002/hlca.19580410640
• 作为产物：
  描述：

  在 肼 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 生成 N-tert-butoxycarbonyl-L-methionine hydrazide
  参考文献：
  名称：

  Design, Synthesis and Biological Evaluation of a Library of Thiocarbazates and Their Activity as Cysteine Protease Inhibitors

  摘要：

  最近，我们鉴定出一类新型高效组织蛋白酶L抑制剂，其特点是具有硫卡巴脒头部结构。鉴于这些化合物有可能抑制其他半胱氨酸蛋白酶，我们设计并合成了一系列硫卡巴脒类化合物，这些化合物在三个位点上含有多样性元素。该化合物的生物活性鉴定结果显示，它们对木瓜蛋白酶家族的半胱氨酸蛋白酶相较于丝氨酸、金属蛋白酶以及某些类别的半胱氨酸蛋白酶（如胱天蛋白酶）表现出显著的选择性。我们鉴定出了几个高效的组织蛋白酶L和S抑制剂。通过对接研究，我们利用SAR数据来理解实现组织蛋白酶S抑制所需的结构要素。这项研究为设计高度有效且选择性的木瓜蛋白酶家族半胱氨酸蛋白酶抑制剂奠定了基础。

  DOI：

  10.2174/138620710791054303

文献信息

• Amino Acid Functionalized Organotin Trichlorides and Their Tin Sulfide Clusters
  作者：Annikka Engel、Stefanie Dehnen

  DOI：10.1002/ejic.201900528

  日期：2019.10.31

  functionalized tin sulfide clusters via organotin trichlorides with boc‐protected amino acids (RAAcSnCl3). In this work we used non‐polar (alanine, valine, leucine, phenylalanine and methionine), polar/neutral (serine and tyrosine) and basic (histidine) amino acids. We obtained single crystals from a Boc‐protected valine derivative of the originally used organotin trichloride R1SnCl3 [R1 = CMe2CH2C(O)Me] and determined

  我们通过有机三氯化锡与boc保护的氨基酸（RAAc SnCl 3）提出了功能化硫化锡簇的新合成方法。在这项工作中，我们使用了非极性（丙氨酸，缬氨酸，亮氨酸，苯丙氨酸和蛋氨酸），极性/中性（丝氨酸和酪氨酸）和碱性（组氨酸）氨基酸。我们从最初使用的有机三氯化锡R 1 SnCl 3 [R 1 = CMe 2 CH 2 C（O）Me]的Boc保护的缬氨酸衍生物中获得了单晶，并通过X射线衍射确定了其结构。随后与硫化物源的反应导致了各种各自的簇结构。通过使用（Me 3 Si）2S或Na 2 S时，反应产物分别为缺陷-异古巴群[[R AAc Sn）3 S 4 Cl]或“多珀德克”型簇[（R AAc Sn）4 S 6 ]，根据119 Sn NMR光谱法。
• Scoffone,E. et al., Gazzetta Chimica Italiana, 1964, vol. 94, p. 695 - 709
  作者：Scoffone,E. et al.

  DOI：——

  日期：——
• Synthesis of 5H-Pyrrolo[3,4-b]pyrazine-Based Peptidomimetics
  作者：Olga Hordiyenko、Angelina Biitseva、Igor Rudenko、Iryna Omelchenko、Axelle Arrault

  DOI：10.1055/s-0035-1560184

  日期：——

  A range of 5H-pyrrolo[3,4-b]pyrazine-based peptidomimetics were designed, and their efficient synthesis starting from 5-imino-5H-pyrrolo[3,4-b]pyrazin-7-amine by subsequent interaction with N-protected amino acid hydrazides and amino acid esters with N,N-carbonyldiimidazole as the coupling agent was elaborated.
• Design, Synthesis and Biological Evaluation of a Library of Thiocarbazates and Their Activity as Cysteine Protease Inhibitors
  作者：Zhuqing Liu、Michael C. Myers、Parag P. Shah、Mary Pat Beavers、Phillip A. Benedetti、Scott L. Diamond、Amos B. Smith,III、Donna M. Huryn

  DOI：10.2174/138620710791054303

  日期：2010.5.1

  Recently, we identified a novel class of potent cathepsin L inhibitors, characterized by a thiocarbazate warhead. Given the potential of these compounds to inhibit other cysteine proteases, we designed and synthesized a library of thiocarbazates containing diversity elements at three positions. Biological characterization of this library for activity against a panel of proteases indicated a significant preference for members of the papain family of cysteine proteases over serine, metallo-, and certain classes of cysteine proteases, such as caspases. Several potent inhibitors of cathepsin L and S were identified. The SAR data were employed in docking studies in an effort to understand the structural elements required for cathepsin S inhibition. This study provides the basis for the design of highly potent and selective inhibitors of the papain family of cysteine proteases.

  最近，我们鉴定出一类新型高效组织蛋白酶L抑制剂，其特点是具有硫卡巴脒头部结构。鉴于这些化合物有可能抑制其他半胱氨酸蛋白酶，我们设计并合成了一系列硫卡巴脒类化合物，这些化合物在三个位点上含有多样性元素。该化合物的生物活性鉴定结果显示，它们对木瓜蛋白酶家族的半胱氨酸蛋白酶相较于丝氨酸、金属蛋白酶以及某些类别的半胱氨酸蛋白酶（如胱天蛋白酶）表现出显著的选择性。我们鉴定出了几个高效的组织蛋白酶L和S抑制剂。通过对接研究，我们利用SAR数据来理解实现组织蛋白酶S抑制所需的结构要素。这项研究为设计高度有效且选择性的木瓜蛋白酶家族半胱氨酸蛋白酶抑制剂奠定了基础。
• Synth�se du N-ac�tyl-L-s�ryl-L-tyrosyl-L-s�ryl-L-m�thionyl-?-L-glutamate de benzyle et de peptides apparent�s
  作者：St. Guttmann、R. A. Boissonnas

  DOI：10.1002/hlca.19580410640

  日期：——

  AbstractN‐CBO‐L‐Seryl‐L‐tyrosyl‐L‐serine methyl ester and L‐methionyl‐γ‐benzyl‐L‐glutamate are prepared by different methods. Condensation by the hydrazideazide procedure affords N‐CBO‐L‐seryl‐L‐tyrosyl‐L‐seryl‐L‐methionyl‐γ‐benzyl‐L‐glutamate, which is shown to be optically pure by leucine‐aminopeptidase digestion. Transformation of the above N‐CBO‐tripeptide ester to the N‐acetyltripeptide ester and condensation by the hydrazide‐azide procedure with the above dipeptide gives N‐acetyl‐L‐seryl‐L‐tyrosyl‐L‐seryl‐L‐methionyl‐γ‐benzyl‐L‐glutamate. The effects produced in the course of fissure of CBO‐ and benzyl‐groups from peptides containing serine and methionine residues, using HBr and acetic acid, are studied.