4-(2-phenylacetoxy)benzyl (tert-butoxycarbonyl)-L-alanyl-L-prolinate | 330970-69-9

• 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: 4-(2-phenylacetoxy)benzyl (tert-butoxycarbonyl)-L-alanyl-L-prolinate
• CAS: 330970-69-9
• 化学式: C₂₈H₃₄N₂O₇
• 分子量: 510.587
• InChiKey: YJVXJNXQAFBDLD-CVDCTZTESA-N

物化性质

• 沸点：
  677.2±55.0 °C(Predicted)
• 密度：
  1.217±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.78
• 重原子数：
  37.0
• 可旋转键数：
  8.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  111.24
• 氢给体数：
  1.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  4-(2-phenylacetoxy)benzyl (tert-butoxycarbonyl)-L-alanyl-L-prolinate 在 immobilized penicillin G acylase (300 U) 作用下， 以 甲醇 、 phosphate buffer 为溶剂， 反应 24.0h， 以81%的产率得到BOC-乙酰氨基异戊酸
  参考文献：
  名称：

  Synthesis and Membrane Binding Properties of a Lipopeptide Fragment from Influenza Virus A Hemagglutinin

  摘要：

  Hemagglutinin from influenza virus A is a S-palmitoylated lipoglycoprotein in which the lipid groups are thought to influence the interaction between cell membrane and capsid during budding of viral offspring as well as fusion processes of the viral membrane with the endosome after entry of the viral particle into the cell. The paper describes the development of a method for the synthesis of characteristic lipidated hemagglutinin derived peptides which additionally carry the fluorescent 7-nitrobenz-2oxa-1,3-diazole (NBD) group. To achieve this goal the enzyme-sensitive para-phenylacetoxybenzyloxycarbonyl (PAOB) ester was developed. It is cleaved from the peptides and lipidated peptides under very mild conditions and with complete selectivity by treatment with the enzyme penicillin G acylase; this results in the formation of a phenolate. This intermediate spontaneously undergoes fragmentation thereby releasing the desired carboxylates. The combined use of this enzymelabile fragmenting ester with the acidlabile Boc group, the Pd-0-sensitive allyl ester and the corresponding Aloc urethane gave access to a mono-S-palmitoylated and a doubly S-palmitoylated NBD-labelled hemagglutinin peptide. The binding of these lipopeptides to model membranes was analyzed in a biophysical setup monitoring the transfer of fluorescent-labelled lipopeptide from vesicles containing the non-ex-changeable fluorescence quencher Rho-DHPE to quencher-free vesicles. The experiments demonstrate that one lipid group is not sufficient for quasi-irreversible membrane insertion of lipidated peptides. This is, however, achieved by introduction of the bis-palmitoyl anchor. The intervesicle transfer always implies release of peptides localized at the outer face of the vesicles into solution followed by diffusion to and insertion into acceptor vesicles. For peptides bound at the inner face of the vesicle membrane, however, an additional flip-flop diffusion to the outer face has to occur beforehand. The kinetics of these processes were estimated by fast chemical quench of the outside fluorophores by sodium dithionite.

  DOI：

  10.1002/1521-3765(20020802)8:15<3362::aid-chem3362>3.0.co;2-0
• 作为产物：
  描述：

  (S)-Pyrrolidine-1,2-dicarboxylic acid 1-tert-butyl ester 2-(4-phenylacetoxy-benzyl) ester 在 盐酸 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二异丙基碳二亚胺 作用下， 以 乙醚 、 二氯甲烷 为溶剂， 反应 17.75h， 生成 4-(2-phenylacetoxy)benzyl (tert-butoxycarbonyl)-L-alanyl-L-prolinate
  参考文献：
  名称：

  Synthesis and Membrane Binding Properties of a Lipopeptide Fragment from Influenza Virus A Hemagglutinin

  摘要：

  Hemagglutinin from influenza virus A is a S-palmitoylated lipoglycoprotein in which the lipid groups are thought to influence the interaction between cell membrane and capsid during budding of viral offspring as well as fusion processes of the viral membrane with the endosome after entry of the viral particle into the cell. The paper describes the development of a method for the synthesis of characteristic lipidated hemagglutinin derived peptides which additionally carry the fluorescent 7-nitrobenz-2oxa-1,3-diazole (NBD) group. To achieve this goal the enzyme-sensitive para-phenylacetoxybenzyloxycarbonyl (PAOB) ester was developed. It is cleaved from the peptides and lipidated peptides under very mild conditions and with complete selectivity by treatment with the enzyme penicillin G acylase; this results in the formation of a phenolate. This intermediate spontaneously undergoes fragmentation thereby releasing the desired carboxylates. The combined use of this enzymelabile fragmenting ester with the acidlabile Boc group, the Pd-0-sensitive allyl ester and the corresponding Aloc urethane gave access to a mono-S-palmitoylated and a doubly S-palmitoylated NBD-labelled hemagglutinin peptide. The binding of these lipopeptides to model membranes was analyzed in a biophysical setup monitoring the transfer of fluorescent-labelled lipopeptide from vesicles containing the non-ex-changeable fluorescence quencher Rho-DHPE to quencher-free vesicles. The experiments demonstrate that one lipid group is not sufficient for quasi-irreversible membrane insertion of lipidated peptides. This is, however, achieved by introduction of the bis-palmitoyl anchor. The intervesicle transfer always implies release of peptides localized at the outer face of the vesicles into solution followed by diffusion to and insertion into acceptor vesicles. For peptides bound at the inner face of the vesicle membrane, however, an additional flip-flop diffusion to the outer face has to occur beforehand. The kinetics of these processes were estimated by fast chemical quench of the outside fluorophores by sodium dithionite.

  DOI：

  10.1002/1521-3765(20020802)8:15<3362::aid-chem3362>3.0.co;2-0

文献信息

• Synthesis and Membrane-Binding Properties of a Characteristic Lipopeptide from the Membrane-Anchoring Domain of Influenza Virus A Hemagglutinin
  作者：Frank Eisele、Jürgen Kuhlmann、Herbert Waldmann

  DOI：10.1002/1521-3773(20010119)40:2<369::aid-anie369>3.0.co;2-7

  日期：2001.1.19

  On the trail of the influenza virus! Fluorescent-labeled lipopeptides, such as the characteristic S-palmitoylated partial structure from influenza virus hemagglutinin A, can be synthesized efficiently by employing a new enzymatic protecting-group technique in the key steps. Their binding to model membranes was determined in a kinetic assay, so leading to a first approximation of the membrane-anchoring ability of the corresponding lipopeptide motif in the parent protein.