| 194737-05-8

• 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
• CAS: 194737-05-8
• 化学式: C₁₄H₁₉N₅O₇
• 分子量: 369.334
• InChiKey: SHOUIQPSOPJJHR-MADCSZMMSA-N

物化性质

• 沸点：
  702.2±60.0 °C(Predicted)
• 密度：
  1.491±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.31
• 重原子数：
  26.0
• 可旋转键数：
  9.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  190.73
• 氢给体数：
  4.0
• 氢受体数：
  8.0

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 、 (2-dodecyl-2-methyl-5-oxooxolan-3-yl) (2R,3R)-2-[[(2R)-2-[[(2R)-2-[[(2S)-2-aminopropanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxybutanoate 在 盐酸 、 水 、 碳酸氢钠 作用下， 以 水 、 丙酮 为溶剂， 反应 1.0h， 生成 、 、
  参考文献：
  名称：

  Isolation, Structure, and Biological Activity of Phaeofungin, a Cyclic Lipodepsipeptide from aPhaeosphaeriasp. Using the Genome-WideCandida albicansFitness Test

  摘要：

  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.

  DOI：

  10.1021/np300704s

文献信息

• Kocurin, the True Structure of PM181104, an Anti-Methicillin-Resistant Staphylococcus aureus (MRSA) Thiazolyl Peptide from the Marine-Derived Bacterium Kocuria palustris
  作者：Jesús Martín、Thiciana da S. Sousa、Gloria Crespo、Sara Palomo、Ignacio González、José Tormo、Mercedes de la Cruz、Matthew Anderson、Russell Hill、Francisca Vicente、Olga Genilloud、Fernando Reyes

  DOI：10.3390/md11020387

  日期：——

  A new thiazolyl peptide, kocurin (1), was isolated from culture broths of a marine-derived Kocuria palustris. Its structural elucidation was accomplished using a combination of spectroscopic and chemical methods, including HRMS, extensive 1D and 2D NMR analysis, MS/MS fragmentation, and chemical degradation and Marfey’s analysis of the resulting amino acid residues. The structure herein reported corrects that previously assigned to PM181104 (3). Kocurin displayed activity against methicillin-resistant Staphylococcus aureus (MRSA), with MIC values in the submicromolar range.

  从一种来源于海洋的 Kocuria palustris 的培养液中分离出了一种新的噻唑肽 Kocurin (1)。利用光谱和化学方法，包括 HRMS、广泛的一维和二维 NMR 分析、MS/MS 片段分析、化学降解以及对所得氨基酸残基的 Marfey 分析，完成了对其结构的阐明。本文报告的结构修正了之前分配给 PM181104 的结构 (3)。Kocurin 对耐甲氧西林金黄色葡萄球菌（MRSA）具有活性，其 MIC 值在亚摩尔范围内。
• 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.