phenacyl (9-fluorenylmethoxycarbonyl)-L-prolylglycolate | 136631-85-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: phenacyl (9-fluorenylmethoxycarbonyl)-L-prolylglycolate
• 英文别名: 1-O-(9H-fluoren-9-ylmethyl) 2-O-(2-oxo-2-phenacyloxyethyl) (2S)-pyrrolidine-1,2-dicarboxylate
• CAS: 136631-85-1
• 化学式: C₃₀H₂₇NO₇
• 分子量: 513.547
• InChiKey: HFJCEYCFFYUMQI-SANMLTNESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5
• 重原子数：
  38
• 可旋转键数：
  11
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  99.2
• 氢给体数：
  0
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  phenacyl (9-fluorenylmethoxycarbonyl)-L-prolylglycolate 在 水 、 溶剂黄146 、 锌 作用下， 以 乙酸乙酯 为溶剂， 反应 16.0h， 生成 O-[N-(9H-fluoren-9-ylmethoxycarbonyl)-L-prolyl]glycolic acid
  参考文献：
  名称：

  Direct cleavage of peptides from a solid support into aqueous buffer. Application in simultaneous multiple peptide synthesis

  摘要：

  A method of simultaneous multiple peptide synthesis which integrates synthesis, side-chain deprotection, cleavage, and purification so as to afford peptide solutions suitable for immediate biological testing is described. The approach utilizes a novel diketopiperazine-forming cleavable linker 1. Upon side-chain deprotection, 1 gives 2, which is stable to a protocol designed to remove contaminants from the support-bound peptide prior to cleavage. Peptide cleavage is then effected by treating 2 with a neutral or near neutral buffer to give peptide 4, which carries a C-terminal diketopiperazine moiety, in good yield. In this study the glycolamido and 4-(oxymethyl)benzamido esters of 1 have been appraised. The approach is demonstrated in model studies on 7 and 8 and in the preparation and characterization of peptides 17-21. The general approach allows 10-100-nmol quantities of many hundreds of peptides to be concurrently prepared in a relatively short period of time when used in conjunction with the multipin method of multiple peptide synthesis.

  DOI：

  10.1021/jo00023a035
• 作为产物：
  描述：

  2-溴苯乙酮 在 4-二甲氨基吡啶 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 二氯甲烷 、 乙酸乙酯 为溶剂， 反应 40.0h， 生成 phenacyl (9-fluorenylmethoxycarbonyl)-L-prolylglycolate
  参考文献：
  名称：

  Direct cleavage of peptides from a solid support into aqueous buffer. Application in simultaneous multiple peptide synthesis

  摘要：

  A method of simultaneous multiple peptide synthesis which integrates synthesis, side-chain deprotection, cleavage, and purification so as to afford peptide solutions suitable for immediate biological testing is described. The approach utilizes a novel diketopiperazine-forming cleavable linker 1. Upon side-chain deprotection, 1 gives 2, which is stable to a protocol designed to remove contaminants from the support-bound peptide prior to cleavage. Peptide cleavage is then effected by treating 2 with a neutral or near neutral buffer to give peptide 4, which carries a C-terminal diketopiperazine moiety, in good yield. In this study the glycolamido and 4-(oxymethyl)benzamido esters of 1 have been appraised. The approach is demonstrated in model studies on 7 and 8 and in the preparation and characterization of peptides 17-21. The general approach allows 10-100-nmol quantities of many hundreds of peptides to be concurrently prepared in a relatively short period of time when used in conjunction with the multipin method of multiple peptide synthesis.

  DOI：

  10.1021/jo00023a035

文献信息

• Simultaneous Multiple Synthesis of Peptide Amides by the Multipin Method. Application of Vapor-Phase Ammonolysis
  作者：Andrew M. Bray、Akhil G. Jhingran、Robert M. Valerio、N. Joe Maeji

  DOI：10.1021/jo00087a041

  日期：1994.4

  A method for simultaneously preparing large numbers of peptide amides is described. Side-chain deprotected, support-bound peptide esters 1 and 2 are incubated with ammonia/tetrahydrofuran vapor. The cleaved peptide amides 3 are then eluted from the support with a solvent of choice. The approach is demonstrated in conjunction with the multipin method of multiple peptide synthesis. In this study, chromophoric model systems of support-bound 4-(oxymethyl)benzamido esters of the genetically coded amino acids (except Cys) 4 and glycolamido esters of Ile, Val and Pro 5 were cleaved using the vapor from solutions of 30% ammonia in tetrahydrofuran) methanol, and 2-propanol. The best yields were obtained with 30% ammonia in tetrahydrofuran. When methanol was used as cosolvent, the amide products were contaminated with methyl ester. When ammonia gas alone was used, very poor yields were recorded. Although the hindered amino acid esters 4(Ile, Val, Pro) cleaved with poor efficiency, the corresponding glycolamido esters S(Ile, Val, Pro) cleaved with >90% efficiency upon treatment with ammonia/tetrahydofuran vapor. Racemization studies on a : selection of dipeptides cleaved by the method demonstrated that only low levels of racemate were generated. Four test peptides 16-19 were prepared and characterized to demonstrate the general utility of the method. The approach gives ready access to hundreds to thousands of discrete peptide amides in quantities (10-100 nmol) sufficient for most biological, immunological, and pharmacological studies.