H-Gln-Val-OBn trifluoroacetate | 87218-90-4

• 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: H-Gln-Val-OBn trifluoroacetate
• 英文别名: H-Gln-Val-OBzl*TFA
• CAS: 87218-90-4
• 化学式: C₂HF₃O₂*C₁₇H₂₅N₃O₄
• 分子量: 449.427
• InChiKey: ZKQLZRLCWAEUEF-SLHAJLBXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  31.0
• 可旋转键数：
  9.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  161.81
• 氢给体数：
  4.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  H-Gln-Val-OBn trifluoroacetate 在 对苯二腈 、 菲 、 palladium 10% on activated carbon 、 氢气 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 1,4-二氧六环 、 水 、 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 6.0h， 生成 tert-butyl N-[(2S)-1-[[(2S)-5-amino-1-[(1-cyano-4-methylpentan-3-yl)amino]-1,5-dioxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]carbamate
  参考文献：
  名称：

  Direct modification of tripeptides using photoinduced decarboxylative radical reactions

  摘要：

  In order to explore the applicability of photoinduced electron transfer (PET) promoted decarboxylative reactions to the direct modification of peptides, a study was performed to assess the influence of amino acid side chains on photoreactions of N-terminal protected tripeptides. Photoinduced decarboxylation reactions of tripeptides, which are composed of central amino acids that possess alkyl, phenyl, thioether, hydroxy, and amide containing side chains, in the presence or absence of acrylonitrile and a thiol were found to proceed smoothly to give the corresponding radical addition, H-abstraction, and substitution products. Although photoreactions of tripeptides containing central amino acids with phenol and indole (Tyr and Trp) moieties do not take place efficiently, appropriate protection of these groups enables the substrates to undergo smooth photoinduced decarboxylative reactions. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2014.12.075
• 作为产物：
  描述：

  L-缬氨酸苄酯对甲苯磺酸盐 在 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 生成 H-Gln-Val-OBn trifluoroacetate
  参考文献：
  名称：

  Direct modification of tripeptides using photoinduced decarboxylative radical reactions

  摘要：

  In order to explore the applicability of photoinduced electron transfer (PET) promoted decarboxylative reactions to the direct modification of peptides, a study was performed to assess the influence of amino acid side chains on photoreactions of N-terminal protected tripeptides. Photoinduced decarboxylation reactions of tripeptides, which are composed of central amino acids that possess alkyl, phenyl, thioether, hydroxy, and amide containing side chains, in the presence or absence of acrylonitrile and a thiol were found to proceed smoothly to give the corresponding radical addition, H-abstraction, and substitution products. Although photoreactions of tripeptides containing central amino acids with phenol and indole (Tyr and Trp) moieties do not take place efficiently, appropriate protection of these groups enables the substrates to undergo smooth photoinduced decarboxylative reactions. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2014.12.075

文献信息

• Amino acids and peptides. VI. Synthesis of the N-terminal pentapeptide of .ALPHA.2-plasmin inhibitor and its analogue.
  作者：SATOSHI OKUSADA、KOICHI KAWASAKI、NOBUTOSHI SUGIYAMA

  DOI：10.1248/cpb.33.3484

  日期：——

  The N-terminal pentapeptide of α2-plasmin inhibitor, H-Asn-Gln-Glu-Gln-Val-OH, and its analogue, H-Asp-Gln-Glu-Gln-Val-OH, were synthesized and their inhibitory effects on the cross-linking reaction of α2-plasmin inhibitor to fibrin mediated by factor XIIIa were examined. The synthetic peptides were inhibitory at high concentration.

  α2-纤溶酶抑制剂的N端五肽H-Asn-Gln-Glu-Gln-Val-OH及其类似物H-Asp-Gln-Glu-Gln-Val-OH被合成，并对其在因子XIIIa介导的α2-纤溶酶抑制剂与纤维蛋白的交联反应中的抑制作用进行了研究。合成的肽在高浓度下具有抑制作用。
• Discovery of novel non-covalent inhibitors selective to the β5-subunit of the human 20S proteasome
  作者：Kai Xu、Ke Wang、Ying Yang、Ding-An Yan、Li Huang、Chin-Ho Chen、Zhiyan Xiao

  DOI：10.1016/j.ejmech.2015.05.023

  日期：2015.6

  A series of linear peptides (6a-6o) were designed based on the known non-covalent 20S proteasome inhibitors TMC-95A and compound 5 via a fragment-based approach. These compounds were synthesized and evaluated against the chymotrypsin-like activity of the human 20S proteasome. Three of them (6d, 6e and 6k) were potent inhibitors with IC50 values at the submicromolar level. These three compounds were selective to the beta 5-subunit and showed no obvious inhibition against trypsin-like and caspase-like activities of the human 20S proteasome. Docking study of the most potent compound 6e revealed its key interactions with the beta 5-subunit of the 20S proteasome. These findings have provided a new chemical template for non-covalent proteasome inhibitors, which is ready for further structural optimization to improve both potency and subunit selectivity. (C) 2015 Elsevier Masson SAS. All rights reserved.