Boc-D-天冬氨酸α-9-芴基甲基酯 | 214630-04-3

• 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
• 中文名称: Boc-D-天冬氨酸α-9-芴基甲基酯
• 英文名称: (3R)-4-(9H-fluoren-9-ylmethoxy)-3-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxobutanoic acid
• CAS: 214630-04-3
• 化学式: C₂₃H₂₅NO₆
• 分子量: 411.455
• InChiKey: RMRKPGGMJKNMSK-LJQANCHMSA-N

物化性质

• 沸点：
  617.4±55.0 °C(Predicted)
• 密度：
  1.251±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.5
• 重原子数：
  30
• 可旋转键数：
  9
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  102
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  BOC-L-亮氨酸 、 Boc-D-缬氨酸 、 BOC-D-色氨酸 、 Boc-D-天冬氨酸α-9-芴基甲基酯 、 alkaline earth salt of/the/ methylsulfuric acid 生成 环(D-ALPHA-天冬氨酰-L-脯氨酰-D-缬氨酰-L-亮氨酰-D-色氨酰)
  参考文献：
  名称：

  Rediscovering an Endothelin Antagonist (BQ-123):  A Self-Deconvoluting Cyclic Pentapeptide Library

  摘要：

  A ''self-deconvoluting'' cyclic pentapeptide library, designed to produce 82 944 head-to-tail-linked peptides in 48 vials, has been prepared. The mixture included amino acids found in a recently optimized endothelin antagonist, BQ-123, originally isolated from microbial sources bg Banyu investigators. Using a positional scan approach, the most potent of 12 residues at each of the four variable positions uniquely rediscovered the BQ-123 sequence or cyclo(L-Pro-D-Val-L-Leu-D-Trp-D-Asp). Resynthesis of the four most potent amino acid combinations gave the following values of relative potency: cyclo(L-Pro-D-Val-L-Leu-D-Trp-D-Asp) or BQ-123 = 1.0, cyclo(L-Pro-D-Pro-L-Leu-D-Trp-D-Asp) = 0.0, cyclo(L-Pro-D-Pro-L-Trp-D-Trp-D-Asp) = 0.0, and cyclo(L-Pro-D-Val-L-Trp-D-Trp-D-Asp) = 0.1. This study reflects the first time that the positional scan approach has been applied to cyclic peptide libraries using a known target, Although no analogs more potent than BQ-123 were discovered, our results provide verification of our synthetic methods for preparing head-to-tail cyclic peptide libraries and also lend support to the use of carefully designed sublibraries for the rapid elucidation of potential leads within a relatively constrained set of peptide macrocycles.

  DOI：

  10.1021/jm9604078
• 作为产物：
  描述：

  Boc-D-天冬氨酸 在 N,N-二异丙基乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 、 乙酸乙酯 为溶剂， 反应 2.0h， 生成 Boc-D-天冬氨酸α-9-芴基甲基酯
  参考文献：
  名称：

  Rediscovering an Endothelin Antagonist (BQ-123):  A Self-Deconvoluting Cyclic Pentapeptide Library

  摘要：

  A ''self-deconvoluting'' cyclic pentapeptide library, designed to produce 82 944 head-to-tail-linked peptides in 48 vials, has been prepared. The mixture included amino acids found in a recently optimized endothelin antagonist, BQ-123, originally isolated from microbial sources bg Banyu investigators. Using a positional scan approach, the most potent of 12 residues at each of the four variable positions uniquely rediscovered the BQ-123 sequence or cyclo(L-Pro-D-Val-L-Leu-D-Trp-D-Asp). Resynthesis of the four most potent amino acid combinations gave the following values of relative potency: cyclo(L-Pro-D-Val-L-Leu-D-Trp-D-Asp) or BQ-123 = 1.0, cyclo(L-Pro-D-Pro-L-Leu-D-Trp-D-Asp) = 0.0, cyclo(L-Pro-D-Pro-L-Trp-D-Trp-D-Asp) = 0.0, and cyclo(L-Pro-D-Val-L-Trp-D-Trp-D-Asp) = 0.1. This study reflects the first time that the positional scan approach has been applied to cyclic peptide libraries using a known target, Although no analogs more potent than BQ-123 were discovered, our results provide verification of our synthetic methods for preparing head-to-tail cyclic peptide libraries and also lend support to the use of carefully designed sublibraries for the rapid elucidation of potential leads within a relatively constrained set of peptide macrocycles.

  DOI：

  10.1021/jm9604078

文献信息

• Rediscovering an Endothelin Antagonist (BQ-123):  A Self-Deconvoluting Cyclic Pentapeptide Library
  作者：Arno F. Spatola、Yvon Crozet、Damiane deWit、Masashi Yanagisawa

  DOI：10.1021/jm9604078

  日期：1996.1.1

  A ''self-deconvoluting'' cyclic pentapeptide library, designed to produce 82 944 head-to-tail-linked peptides in 48 vials, has been prepared. The mixture included amino acids found in a recently optimized endothelin antagonist, BQ-123, originally isolated from microbial sources bg Banyu investigators. Using a positional scan approach, the most potent of 12 residues at each of the four variable positions uniquely rediscovered the BQ-123 sequence or cyclo(L-Pro-D-Val-L-Leu-D-Trp-D-Asp). Resynthesis of the four most potent amino acid combinations gave the following values of relative potency: cyclo(L-Pro-D-Val-L-Leu-D-Trp-D-Asp) or BQ-123 = 1.0, cyclo(L-Pro-D-Pro-L-Leu-D-Trp-D-Asp) = 0.0, cyclo(L-Pro-D-Pro-L-Trp-D-Trp-D-Asp) = 0.0, and cyclo(L-Pro-D-Val-L-Trp-D-Trp-D-Asp) = 0.1. This study reflects the first time that the positional scan approach has been applied to cyclic peptide libraries using a known target, Although no analogs more potent than BQ-123 were discovered, our results provide verification of our synthetic methods for preparing head-to-tail cyclic peptide libraries and also lend support to the use of carefully designed sublibraries for the rapid elucidation of potential leads within a relatively constrained set of peptide macrocycles.