L-Serine,N-[5-[[1-(aminocarbonyl)-2-methylpropyl]amino]-2,4-dinitrophenyl]-, (S)- | 137817-22-2

• 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: L-Serine,N-[5-[[1-(aminocarbonyl)-2-methylpropyl]amino]-2,4-dinitrophenyl]-, (S)-
• 英文别名: L-Ser-L-FDVA
• CAS: 137817-22-2
• 化学式: C₁₄H₁₉N₅O₈
• 分子量: 385.334
• InChiKey: GTFUSISQODLLAC-CABZTGNLSA-N

物化性质

• 沸点：
  764.6±60.0 °C(Predicted)
• 密度：
  1.571±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.28
• 重原子数：
  27.0
• 可旋转键数：
  10.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  210.96
• 氢给体数：
  5.0
• 氢受体数：
  9.0

反应信息

• 作为产物：
  描述：

  Nα-(2,4-二硝基-5-氟苯基)-L-缬氨酰胺 、 tsukubachelin 在 水 、 氢碘酸 、 碳酸氢钠 作用下， 以 丙酮 为溶剂， 反应 16.05h， 生成 L-Serine,N-[5-[[1-(aminocarbonyl)-2-methylpropyl]amino]-2,4-dinitrophenyl]-, (S)- 、
  参考文献：
  名称：

  从 Streptomyces sp. 中分离出的一种新的铁载体。TM-34 对血管紧张素转换酶具有强效抑制活性

  摘要：

  从新分离菌株 Streptomyces sp. 的缺铁培养基中分离出一种名为 tsukubachelin 的新铁载体。TM-34。tsukubachelin 的化学结构是通过 2D NMR 和 TOF-Mass 光谱数据的解释确定的。tsukubachelin 的结构由 6 个氨基酸残基组成，包括 3 个丝氨酸，N-α-甲基-N-δ-羟基-N-δ-甲酰鸟氨酸、N-α-甲基-N-δ-羟基鸟氨酸各一个，以及环状N-羟基鸟氨酸。因为据报道结构相关的铁载体去铁-foroximithine 具有强效的血管紧张素转换酶抑制活性，所以测试了去铁-tsukubachelin 和去铁-foroximithine 的抑制活性以进行结构-活性比较。Desferri-tsukubachelin 显示出比去铁-foroximithine 强 14 倍的抑制活性。

  DOI：

  10.1002/ejoc.201100189

文献信息

• Krisynomycins, Imipenem Potentiators against Methicillin-Resistant <i>Staphylococcus aureus</i>, Produced by <i>Streptomyces canus</i>
  作者：Mercedes Pérez-Bonilla、Daniel Oves-Costales、Ignacio González、Mercedes de la Cruz、Jesús Martín、Francisca Vicente、Olga Genilloud、Fernando Reyes

  DOI：10.1021/acs.jnatprod.0c00294

  日期：2020.9.25

  A reinvestigation of the acetone extract of the strain CA-091830 of Streptomyces canus, producer of the imipenem potentiator krisynomycin, resulted in the isolation of two additional analogues, krisynomycins B (1) and C (2), with different chlorination patterns. Genome sequencing of the strain followed by detailed bioinformatics analysis led to the identification of the corresponding biosynthetic gene cluster (BGC) of this cyclic nonribosomal peptide family. The planar structure of the new molecules was determined using HRMS, ESI-qTOF-MS/MS, and 1D and 2D NMR data. Their absolute configuration was proposed using a combination of Marfey's and bioinformatic BGC analyses. The krisynomycins displayed weak to negligible antibiotic activity against methicillin-resistant Staphylococcus aureus (MRSA), which was significantly enhanced when tested in combination with sublethal concentrations of imipenem. The halogenation pattern plays a key role in the antimicrobial activity and imipenem-potentiating effects of the compounds, with molecules having a higher number of chlorine atoms potentiating the effect of imipenem at lower doses.
• Isolation, Structure, and Biological Activity of Phaeofungin, a Cyclic Lipodepsipeptide from a<i>Phaeosphaeria</i>sp. Using the Genome-Wide<i>Candida albicans</i>Fitness Test
  作者：Sheo B. Singh、John Ondeyka、Guy Harris、Kithsiri Herath、Deborah Zink、Francisca Vicente、Gerald Bills、Javier Collado、Gonzalo Platas、Antonio González del Val、Jesus Martin、Fernando Reyes、Hao Wang、Jennifer Nielsen Kahn、Stefan Galuska、Robert Giacobbe、George Abruzzo、Terry Roemer、Deming Xu

  DOI：10.1021/np300704s

  日期：2013.3.22

  Phaeofungin (1), a new cyclic depsipeptide isolated from Phaeosphaeria sp., was discovered by application of reverse genetics technology, using the Candida albicans fitness test (CaFT). Phaeofungin is comprised of seven amino acids and a beta,gamma-dihydroxy-gamma-methylhexadecanoic acid arranged in a 25-membered cyclic depsipeptide. Five of the amino acids were assigned with D-configurations. The structure was elucidated by 2D-NMR and HRMS-MS analysis of the natural product and its hydrolyzed linear peptide. The absolute configuration of the amino acids was determined by Marfey's method by complete and partial hydrolysis of 1. The CaFT profile of the phaeofungin-containing extract overlapped with that of phomafungin (3), another structurally different cyclic lipodepsipeptide isolated from a Phoma sp. using the same approach. Comparative biological characterization further demonstrated that these two fungal lipodepsipeptides are functionally distinct. While phomafungin was potentiated by cyclosporin A (an inhibitor of the calcineurin pathway), phaeofungin was synergized with aureobasidin A (2) (an inhibitor of the sphingolipid biosynthesis) and to some extent caspofungin (an inhibitor of glucan synthase). Furthermore, phaeofiingin caused ATP release in wild-type C. albicans strains but phomafungin did not. It showed modest antifungal activity against C. albicans (MIC 16-32 mu g/mL) and better activity against Aspergillus fumigatus (MIC 8-16 mu g/mL) and Trichophyton mentagrophytes (MIC 4 mu g/mL). The linear peptide was inactive, suggesting that the macrocyclic depsipeptide ring is essential for target engagement and antifungal activity.