N-(3-aminopropyl)-4-benzoylbenzamide | 1352438-92-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: N-(3-aminopropyl)-4-benzoylbenzamide
• CAS: 1352438-92-6
• 化学式: C₁₇H₁₈N₂O₂
• 分子量: 282.342
• InChiKey: WMUMVCIHCVMEKW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.6
• 重原子数：
  21
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.18
• 拓扑面积：
  72.2
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N-(3-aminopropyl)-4-benzoylbenzamide 、 在 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 1-羟基苯并三唑 、 N,N-二异丙基乙胺 作用下， 以 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 16.0h， 以7%的产率得到(1S,2R,18R,19R,22S,25R,28R,40S)-22-(2-amino-2-oxoethyl)-N-[3-[(4-benzoylbenzoyl)amino]propyl]-5,15-dichloro-48-[(2S,3R,4S,5S,6R)-3-[(2S,4S,5S,6S)-4-(hex-5-ynoylamino)-5-hydroxy-4,6-dimethyloxan-2-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-2,18,32,35,37-pentahydroxy-19-[[(2R)-4-methyl-2-(methylamino)pentanoyl]amino]-20,23,26,42,44-pentaoxo-7,13-dioxa-21,24,27,41,43-pentazaoctacyclo[26.14.2.23,6.214,17.18,12.129,33.010,25.034,39]pentaconta-3,5,8(48),9,11,14,16,29(45),30,32,34(39),35,37,46,49-pentadecaene-40-carboxamide
  参考文献：
  名称：

  Unraveling the Protein Targets of Vancomycin in Living S. aureus and E. faecalis Cells

  摘要：

  Vancomycin is a potent glycopeptide antibiotic that has evolved to specifically bind to the D-Ala-D-Ala dipeptide termini of nascent peptidoglycans. Although this mode of action is well established, several studies indicate that vancomycin and analogues exploit noncanonical target sites. In order to address all vancomycin targets in clinically relevant Staphylococcus aureus and Enterococcus faecalis strains we developed a series of small-molecule photoaffinity probes based on vancomycin. Proteomic profiling revealed the specific labeling of two previously unknown vancomycin targets that are likely to contribute to its antibiotic activity. The specific inhibition of the major staphylococcal autolysin Atl confirms previous observations that vancomycin alters S. aureus cell morphology by interaction with the autolytic machinery. Moreover, in E. faecalis the vancomycin photoprobe specifically binds to an ABC transporter protein, which likely impedes the uptake of essential nutrients such as sugars and peptides. The labeling of these two prominent membrane targets in living cells reveals a thus far unexplored mode of vancomycin binding and inhibition that could allow a rational design of variants with improved activity.

  DOI：

  10.1021/ja2039979
• 作为产物：
  描述：

  3-苯甲酰苯甲酸 、 1,3-丙二胺 在 4-二甲氨基吡啶 、 N,N'-二异丙基碳二亚胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 2.17h， 以72%的产率得到N-(3-aminopropyl)-4-benzoylbenzamide
  参考文献：
  名称：

  Unraveling the Protein Targets of Vancomycin in Living S. aureus and E. faecalis Cells

  摘要：

  Vancomycin is a potent glycopeptide antibiotic that has evolved to specifically bind to the D-Ala-D-Ala dipeptide termini of nascent peptidoglycans. Although this mode of action is well established, several studies indicate that vancomycin and analogues exploit noncanonical target sites. In order to address all vancomycin targets in clinically relevant Staphylococcus aureus and Enterococcus faecalis strains we developed a series of small-molecule photoaffinity probes based on vancomycin. Proteomic profiling revealed the specific labeling of two previously unknown vancomycin targets that are likely to contribute to its antibiotic activity. The specific inhibition of the major staphylococcal autolysin Atl confirms previous observations that vancomycin alters S. aureus cell morphology by interaction with the autolytic machinery. Moreover, in E. faecalis the vancomycin photoprobe specifically binds to an ABC transporter protein, which likely impedes the uptake of essential nutrients such as sugars and peptides. The labeling of these two prominent membrane targets in living cells reveals a thus far unexplored mode of vancomycin binding and inhibition that could allow a rational design of variants with improved activity.

  DOI：

  10.1021/ja2039979

文献信息

• Composition and method for preparing biocompatible surfaces
  申请人：SurModics, Inc.

  公开号：EP2329852A1

  公开（公告）日：2011-06-08

  The invention provides methods and compositions for providing biocompatible surfaces to medical articles. In particular the invention provides biocompatible coatings with heparin activity. In some aspects the biocompatible coating of the invention are able to release a bioactive agent. The coatings can be formed using biostable or biodegradable polymeric material and photoreactive groups. The invention also provides methods for improving the quality of bioactive agent-containing coatings by performing pre-irradiation of biocompatible coating compositions.

  本发明提供了为医疗用品提供生物相容性表面的方法和组合物。本发明尤其提供了具有肝素活性的生物相容性涂层。在某些方面，本发明的生物相容性涂层能够释放生物活性剂。这些涂层可以使用生物稳定或可生物降解的聚合物材料和光活性基团形成。本发明还提供了通过对生物相容性涂层组合物进行预辐照来提高含生物活性剂涂层质量的方法。
• Unraveling the Protein Targets of Vancomycin in Living S. aureus and E. faecalis Cells
  作者：Jürgen Eirich、Ronald Orth、Stephan A. Sieber

  DOI：10.1021/ja2039979

  日期：2011.8.10

  Vancomycin is a potent glycopeptide antibiotic that has evolved to specifically bind to the D-Ala-D-Ala dipeptide termini of nascent peptidoglycans. Although this mode of action is well established, several studies indicate that vancomycin and analogues exploit noncanonical target sites. In order to address all vancomycin targets in clinically relevant Staphylococcus aureus and Enterococcus faecalis strains we developed a series of small-molecule photoaffinity probes based on vancomycin. Proteomic profiling revealed the specific labeling of two previously unknown vancomycin targets that are likely to contribute to its antibiotic activity. The specific inhibition of the major staphylococcal autolysin Atl confirms previous observations that vancomycin alters S. aureus cell morphology by interaction with the autolytic machinery. Moreover, in E. faecalis the vancomycin photoprobe specifically binds to an ABC transporter protein, which likely impedes the uptake of essential nutrients such as sugars and peptides. The labeling of these two prominent membrane targets in living cells reveals a thus far unexplored mode of vancomycin binding and inhibition that could allow a rational design of variants with improved activity.