(2S)-2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-(2'-methoxyphenyl)propionic acid tert-butyl ester | 381222-41-9

• 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: (2S)-2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-(2'-methoxyphenyl)propionic acid tert-butyl ester
• 英文别名: tert-butyl (2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-(2-methoxyphenyl)propanoate
• CAS: 381222-41-9
• 化学式: C₂₉H₃₁NO₅
• 分子量: 473.569
• InChiKey: HTFOOEWFDWTMOZ-VWLOTQADSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.9
• 重原子数：
  35
• 可旋转键数：
  10
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  73.9
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (2S)-2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-(2'-methoxyphenyl)propionic acid tert-butyl ester 在 二乙胺 作用下， 以 二氯甲烷 为溶剂， 生成 (S)-tert-butyl-2-amino-3-(2-methoxyphenyl)propanoate
  参考文献：
  名称：

  Toward a Rational Design of Peptide Inhibitors of Ribonucleotide Reductase:  Structure−Function and Modeling Studies

  摘要：

  Mammalian ribonucleotide reductase, a chemotherapeutic target, has two subunits, mR1 and mR2, and is inhibited by AcF(1)TLDADF(7), denoted P7. P7 corresponds to the C-terminus of mR2 and competes with mR2 for binding to mR1. We report results of a structure-function analysis of P7, obtained using a new assay measuring peptide ligand binding to mR1, that demonstrate stringent specificity for Phe at F-7, high specificity for Phe at F-1, and little specificity for the N-acyl group. They support a structural model in which the dominant interactions of P7 occur at two mR1 sites, the F-1 and F-7 subsites. The model is constructed from the structure of Escherichia colt R1 (eR1) complexed with the C-terminal peptide from eR2, aligned sequences of mR1 and eR1, and the trNOE-derived structure of mR1-bound P7. Comparison of this model with similar models constructed for mR1 complexed with other inhibitory ligands indicates that increased F-1 subsite interaction can offset lower F-7 subsite interaction and suggests strategies for the design of new, higher affinity inhibitors.

  DOI：

  10.1021/jm000335r
• 作为产物：
  描述：

  Fmoc-β-氯-L-丙氨酸 在 三甲基氯硅烷 、 硫酸 、 sodium iodide 、 锌 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 、 丙酮 为溶剂， 反应 95.0h， 生成 (2S)-2-(9H-Fluoren-9-ylmethoxycarbonylamino)-3-(2'-methoxyphenyl)propionic acid tert-butyl ester
  参考文献：
  名称：

  使用有机锌化学方法直接合成Fmoc保护的氨基酸：应用于聚甲氧基化的苯丙氨酸和4-氧代氨基酸

  摘要：

  新型N -Fmoc 3-碘丙氨酸叔丁酯衍生的有机锌试剂1，从光学纯品中分7步获得大号丝氨酸，在钯催化下与一系列亲电试剂偶联，以可变的收率（21-59％）得到取代的苯丙氨酸和4-氧代氨基酸。转化为有机铜试剂13允许与烯丙基氯 和 草酰氯乙酯。拆除叔丁基 提供Fmoc保护 氨基酸 （63–95％），适用于自动化固相 肽 合成。

  DOI：

  10.1039/b103832j

文献信息

• Toward a Rational Design of Peptide Inhibitors of Ribonucleotide Reductase:  Structure−Function and Modeling Studies
  作者：Bari A. Pender、Xu Wu、Paul H. Axelsen、Barry S. Cooperman

  DOI：10.1021/jm000335r

  日期：2001.1.1

  Mammalian ribonucleotide reductase, a chemotherapeutic target, has two subunits, mR1 and mR2, and is inhibited by AcF(1)TLDADF(7), denoted P7. P7 corresponds to the C-terminus of mR2 and competes with mR2 for binding to mR1. We report results of a structure-function analysis of P7, obtained using a new assay measuring peptide ligand binding to mR1, that demonstrate stringent specificity for Phe at F-7, high specificity for Phe at F-1, and little specificity for the N-acyl group. They support a structural model in which the dominant interactions of P7 occur at two mR1 sites, the F-1 and F-7 subsites. The model is constructed from the structure of Escherichia colt R1 (eR1) complexed with the C-terminal peptide from eR2, aligned sequences of mR1 and eR1, and the trNOE-derived structure of mR1-bound P7. Comparison of this model with similar models constructed for mR1 complexed with other inhibitory ligands indicates that increased F-1 subsite interaction can offset lower F-7 subsite interaction and suggests strategies for the design of new, higher affinity inhibitors.
• Direct synthesis of Fmoc-protected amino acids using organozinc chemistry: application to polymethoxylated phenylalanines and 4-oxoamino acids†
  作者：Hervé J. C. Deboves、Christian A. G. N. Montalbetti、Richard F. W. Jackson

  DOI：10.1039/b103832j

  日期：——

  organozinc reagent 1, obtained in 7 steps from optically pure L-serine, was coupled to a range of electrophiles under palladium catalysis to give substituted phenylalanines and 4-oxoamino acids in variable yields (21–59%). Transformation into the organocopper reagent 13 allowed coupling with allyl chloride and ethyl oxalyl chloride. Removal of the tert-butyl group gives Fmoc-protected amino acids (63–95%)

  新型N -Fmoc 3-碘丙氨酸叔丁酯衍生的有机锌试剂1，从光学纯品中分7步获得大号丝氨酸，在钯催化下与一系列亲电试剂偶联，以可变的收率（21-59％）得到取代的苯丙氨酸和4-氧代氨基酸。转化为有机铜试剂13允许与烯丙基氯 和 草酰氯乙酯。拆除叔丁基 提供Fmoc保护 氨基酸 （63–95％），适用于自动化固相 肽 合成。