NH2-(Boc)Lys-NMe-D-Phe-Phe-(Cbz)Lys-Leu-OH | 1321841-92-2

• 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: NH2-(Boc)Lys-NMe-D-Phe-Phe-(Cbz)Lys-Leu-OH
• CAS: 1321841-92-2
• 化学式: C₅₀H₇₁N₇O₁₀
• 分子量: 930.155
• InChiKey: SYAZHGJSWUATLN-VYFGVMMVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.0
• 重原子数：
  67.0
• 可旋转键数：
  27.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  247.59
• 氢给体数：
  7.0
• 氢受体数：
  10.0

反应信息

• 作为反应物：
  描述：

  NH2-(Boc)Lys-NMe-D-Phe-Phe-(Cbz)Lys-Leu-OH 在 O-(benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 、 N,N-二异丙基乙胺 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 、 3-(二乙氧基邻酰氧基)-1,2,3-苯并三嗪-4-酮 作用下， 以 二氯甲烷 、 乙腈 为溶剂， 以10%的产率得到macrocycle (Boc)Lys-NMe-D-Phe-Phe-(Cbz)Lys-Leu
  参考文献：
  名称：

  Synthesis and evaluation of biotinylated sansalvamide A analogs and their modulation of Hsp90

  摘要：

  Described are the syntheses of three sansalvamide A derivatives that contain biotinylated tags at individual positions around the macrocycle. The tagged derivatives indicated in protein pull-down assays that they bind to Hsp90 at the same binding site (N-Middle domain) as the San A-amide peptide. Further, these compounds inhibit binding between Hsp90 and multiple C-terminal client proteins. This interaction is unique to the San A analogs indicating they can be tuned for selectivity against Hsp90 client/ co-chaperone proteins. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.06.083
• 作为产物：
  描述：

  2-chlorotrityl-leucine resin 、 N'-芴甲氧羰基-N-苄氧羰基-L-赖氨酸 、 Fmoc-L-苯丙氨酸 、 N-alpha-芴甲氧羰基-N-epsilon-叔丁氧羰基-L-赖氨酸 、 N-芴甲氧羰酰基-N-甲基-D-苯丙氨酸 在 1-羟基苯并三唑 、 N,N'-二异丙基碳二亚胺 、 哌啶 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以706 mg的产率得到NH2-(Boc)Lys-NMe-D-Phe-Phe-(Cbz)Lys-Leu-OH
  参考文献：
  名称：

  Synthesis and evaluation of biotinylated sansalvamide A analogs and their modulation of Hsp90

  摘要：

  Described are the syntheses of three sansalvamide A derivatives that contain biotinylated tags at individual positions around the macrocycle. The tagged derivatives indicated in protein pull-down assays that they bind to Hsp90 at the same binding site (N-Middle domain) as the San A-amide peptide. Further, these compounds inhibit binding between Hsp90 and multiple C-terminal client proteins. This interaction is unique to the San A analogs indicating they can be tuned for selectivity against Hsp90 client/ co-chaperone proteins. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.06.083