Boc-L-Ala-γ-D-Glu(OMe)-OH | 79334-92-2

• 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: Boc-L-Ala-γ-D-Glu(OMe)-OH
• 英文别名: Boc-Ala-D-iso-Glu(OMe)-OH；Boc-L-Ala-D-Glu(OH)OMe；(4R)-5-methoxy-4-[[(2S)-2-[(2-methylpropan-2-yl)oxycarbonylamino]propanoyl]amino]-5-oxopentanoic acid
• CAS: 79334-92-2
• 化学式: C₁₄H₂₄N₂O₇
• 分子量: 332.354
• InChiKey: BOQIRHPKPHJWKK-DTWKUNHWSA-N

物化性质

• 沸点：
  555.1±50.0 °C(Predicted)
• 密度：
  1.200±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.5
• 重原子数：
  23
• 可旋转键数：
  10
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  131
• 氢给体数：
  3
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  Boc-L-Ala-γ-D-Glu(OMe)-OH 在 盐酸 、 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 、 二氯甲烷 为溶剂， 反应 13.0h， 生成 H-Ala-(D)-iso-Glu-(OMe)-Lys-(N^ε-COCF3)-(D)-Ala-(D)-Ala-OMe
  参考文献：
  名称：

  N-Methylimidazolium chloride-catalyzed pyrophosphate formation: Application to the synthesis of Lipid I and NDP-sugar donors

  摘要：

  N-Methylimidazolium chloride is found to catalyze a coupling reaction between monophosphates and activated phosphorous-nitrogen intermediates such as a phosphorimidazolide and phosphoromorpholidate to form biologically important unsymmetrical pyrophosphate diesters. The catalyst is much more active, cheaper, and less explosive than 1H-tetrazole, known as the best catalyst for the pyrophosphate formation over a decade. The mild and neutral reaction conditions are compatible with allylic pyrophosphate formation in Lipid I syntheisis. (31)P NMR experiments suggest that the catalyst acts not only as an acid but also as a nucleophile to form cationic and electrophilic phosphor-N-methylimidazolide intermediates in the pyrophosphate formation. (c) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.04.061
• 作为产物：
  描述：

  N-[N-[叔丁氧羰基]-L-丙氨酰基]-D-谷氨酸 5-苄基酯 在 palladium 10% on activated carbon 、 氢气 作用下， 以 甲醇 、 乙醚 、 正己烷 、 乙酸乙酯 为溶剂， 反应 12.5h， 生成 Boc-L-Ala-γ-D-Glu(OMe)-OH
  参考文献：
  名称：

  Transpeptidase-Mediated Incorporation of d-Amino Acids into Bacterial Peptidoglycan

  摘要：

  The beta-lactams are the most important class of antibiotics in clinical use. Their lethal targets are the transpeptidase domains of penicillin binding proteins (PBPs), which catalyze the cross-linking of bacterial peptidoglycan (PG) during cell wall synthesis. The transpeptidation reaction occurs in two steps, the first being formation of a covalent enzyme intermediate and the second involving attack of an amine on this intermediate. Here we use defined PG substrates to dissect the individual steps catalyzed by a purified E. coli transpeptidase. We demonstrate that this transpeptidase accepts a set of structurally diverse D-amino acid substrates and incorporates them into PG fragments. These results provide new information on donor and acceptor requirements as well as a mechanistic basis for previous observations that noncanonical D-amino acids can be introduced into the bacterial cell wall.

  DOI：

  10.1021/ja2040656

文献信息

• Peptide, process for preparation thereof and use thereof
  申请人：Fujisawa Pharmaceutical Company, Ltd.

  公开号：US04725582A1

  公开（公告）日：1988-02-16

  The invention concerns peptides, having the pharmaceutical property of enhancing the immune response, having the structure: ##STR1## wherein R.sup.1 is alkanoyl, R.sub.b.sup.1 is hydrogen, methyl, isopropyl, hydroxymethyl, protected hydroxymethyl or benzyl, R.sup.2 is hydrogen, carboxy, protected carboxy or a group of the formula: ##STR2## wherein R.sub.a.sup.2 is mono- or di-carboxy (or protected carboxy) lower alkyl or ar(carboxy or protected carboxy) lower alkyl whose aryl moiety is substituted by hydroxy or not substituted, R.sub.b.sup.2 is hydrogen or lower alkyl, R.sup.p is hydrogen, carboxy or protected carboxy, R.sup.q is carboxy, protected carboxy or a group of the formula ##STR3## wherein R.sub.a.sup.2 and R.sub.b.sup.2 are each as defined above, R.sup.r is hydrogen or amino protective group, m is an integer 1 to 3, and n is an integer 1.

  本发明涉及一种具有增强免疫反应药物性质的肽，其结构为：##STR1## 其中，R.sup.1是脂肪酰基，R.sub.b.sup.1是氢、甲基、异丙基、羟甲基、保护羟甲基或苄基，R.sup.2是氢、羧基、保护羧基或式：##STR2## 其中，R.sub.a.sup.2是单或双羧基（或保护羧基）较低烷基或芳（羧基或保护羧基）较低烷基，其芳基部分被羟基取代或未取代，R.sub.b.sup.2是氢或较低烷基，R.sup.p是氢、羧基或保护羧基，R.sup.q是羧基、保护羧基或式：##STR3## 其中，R.sub.a.sup.2和R.sub.b.sup.2的含义与上述相同，R.sup.r是氢或氨基保护基，m是1至3的整数，n是1。
• Oxazole derivatives
  申请人：Fujisawa Pharmaceutical Company, Ltd.

  公开号：US04458078A1

  公开（公告）日：1984-07-03

  The invention relates to novel intermediates for the preparation of peptides of pharmacological activity, said intermediates being of the formulas: ##STR1## wherein R.sub.2.sup.r is amino protective group and Y is hydrogen or amino protective group; and : ##STR2##

  本发明涉及用于制备具有药理活性的肽的新型中间体，所述中间体的化学式为：##STR1## 其中R.sub.2.sup.r是氨基保护基，Y是氢或氨基保护基；以及：##STR2##
• New peptide, process for preparation thereof and use thereof
  申请人：Fuisawa Pharmaceutical Company, Ltd.

  公开号：US04539155A1

  公开（公告）日：1985-09-03

  The invention relates to compounds and salts of compounds which are diaminopimelyl peptides, N-acetoxypropionyl or N-t-butoxycarbonyl-amino-acid - (.alpha.-OBzl) glutamic acid peptides or N-acylated derivatives of (.alpha.-OBzl) glytamic acid or of (.alpha.-OBzl) aminoadipic acid. The compounds and their salts are starting materials for the preparation of pharmacologically active peptides.

  本发明涉及具有二氨基戊二酰基肽、N-乙酰氧丙酰基或N-t-叔丁氧羰基氨基酸-(α-OBzl)谷氨酸肽或(α-OBzl)氨基己二酸的N-酰化衍生物的化合物和盐。这些化合物及其盐是制备药理活性肽的起始物料。
• Synthetic tripeptides as alternate substrates of murein peptide ligase (Mpl)
  作者：Mireille Hervé、Andreja Kovač、Cécile Cardoso、Delphine Patin、Boris Brus、Hélène Barreteau、Dominique Mengin-Lecreulx、Stanislav Gobec、Didier Blanot

  DOI：10.1016/j.biochi.2012.12.011

  日期：2013.6

  Murein peptide ligase (Mpl) is an enzyme found in Gram-negative bacteria. It catalyses the addition of tripeptide L-Ala-gamma-D-Glu-meso-diaminopimelate to nucleotide precursor UDP-N-acetylmuramic acid during the recycling of peptidoglycan. Although not essential, this enzyme represents an interesting target for antibacterial compounds through the synthesis of alternate substrates whose incorporation into peptidoglycan might be deleterious for the bacterial cell. Therefore, we have synthesised 10 tripeptides L-Ala-gamma-D-Glu-Xaa in which Xaa represents amino acids different from diaminopimelic acid. Tripeptide with Xaa = epsilon-D-Lys proved to be an excellent substrate of Escherichia coli Mpl in vitro. Tripeptides with Xaa = p-amino- or p-nitro-L-phenylalanine were poor substrates, while tripeptides with Xaa = D- or L-2-aminopimelate, DL-2-aminoheptanoic acid, L-Glu, L-norleucine, L-norvaline, L-2-aminobutyric acid or L-Ala were not substrates at all. Although a good Mpl substrate, the D-Lys-containing tripeptide was devoid of antibacterial activity against E. coli, presumably owing to poor uptake. (C) 2012 Elsevier Masson SAS. All rights reserved.
• Forming Cross-Linked Peptidoglycan from Synthetic Gram-Negative Lipid II
  作者：Matthew D. Lebar、Tania J. Lupoli、Hirokazu Tsukamoto、Janine M. May、Suzanne Walker、Daniel Kahne

  DOI：10.1021/ja312510m

  日期：2013.3.27

  The bacterial cell wall precursor, Lipid II, has a highly conserved structure among different organisms except for differences in the amino acid sequence of the peptide side chain. Here, we report an efficient and flexible synthesis of the canonical Lipid II precursor required for the assembly of Gram-negative peptidoglycan (PG). We use a rapid LC/MS assay to analyze PG glycosyltransfer (PGT) and transpeptidase (TP) activities of Escherichia coli penicillin binding proteins PBP1A and PBP1B and show that the native m-DAP residue in the peptide side chain of Lipid II is required in order for TP-catalyzed peptide cross-linking to occur in vitro. Comparison of PG produced from synthetic canonical E. coli Lipid II with PG isolated from E. coli cells demonstrates that we can produce PG in vitro that resembles native structure. This work provides the tools necessary for reconstituting cell wall synthesis, an essential cellular process and major antibiotic target, in a purified system.