NH2-Lys(Cbz)-Lys(Boc)-Val-N-Me-D-Phe-Phe-OH | 1321842-01-6

• 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-Lys(Cbz)-Lys(Boc)-Val-N-Me-D-Phe-Phe-OH
• 英文别名: NH2-(Cbz)Lys-(Boc)Lys-Val-NMe-D-Phe-Phe-OH
• CAS: 1321842-01-6
• 化学式: C₄₉H₆₉N₇O₁₀
• 分子量: 916.128
• InChiKey: FPTLRXXSTMVWMO-IURJAOHMSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.61
• 重原子数：
  66.0
• 可旋转键数：
  26.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.49
• 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-Lys(Cbz)-Lys(Boc)-Val-N-Me-D-Phe-Phe-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-) 、 三氟乙酸 、 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， 生成 macrocycle (Cbz)Lys-lys(Peg-Biotin)-Val-NMe-D-Phe-Phe
  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：

  H-Phe-2-ClTrt resin 、 Fmoc-L-缬氨酸 、 N'-芴甲氧羰基-N-苄氧羰基-L-赖氨酸 、 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340 mg的产率得到NH2-Lys(Cbz)-Lys(Boc)-Val-N-Me-D-Phe-Phe-OH
  参考文献：
  名称：

  A small molecule that preferentially binds the closed conformation of Hsp90

  摘要：

  Described is the synthesis of three different fluorescein-tagged derivatives of a macrocycle, and their binding affinity to heat shock protein 90 (Hsp90). Using fluorescence polarization anisotropy, we report the binding affinity of these fluorescein-labeled compounds to Hsp90 in its open state and ATP-dependent closed state. We show that the compounds demonstrate a conformation-dependent preference for binding to the closed state. Published by Elsevier Ltd.

  DOI：

  10.1016/j.bmcl.2011.09.096