N-Boc-L-Ser-Ile-OH | 145435-25-2

• 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: N-Boc-L-Ser-Ile-OH
• 英文别名: Boc-Ser-Ile-OH
• CAS: 145435-25-2
• 化学式: C₁₄H₂₆N₂O₆
• 分子量: 318.37
• InChiKey: FQVISSIQBVDBIZ-GUBZILKMSA-N

物化性质

• 沸点：
  559.6±50.0 °C(Predicted)
• 密度：
  1.174±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.49
• 重原子数：
  22.0
• 可旋转键数：
  7.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.79
• 拓扑面积：
  124.96
• 氢给体数：
  4.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  (4-hydroxyphenyl)(methyl)(benzyl)sulfonium chloride 、 N-Boc-L-Ser-Ile-OH 在 potassium carbonate 作用下， 以 二氯甲烷 为溶剂， 反应 8.0h， 以74%的产率得到
  参考文献：
  名称：

  Peptide Synthesis in Aqueous Solution. V. Properties and Reactivities of (p-Hydroxyphenyl)benzylmethylsulfonium Salts for Direct Benzyl Esterification ofN-Acylpeptides

  摘要：

  制备了一些（对羟基苯基）苄基甲基硫盐。这些化合物生成了苄基阳离子，并且不仅将N-酰基氨基酸，还将N-酰基肽转化为其相应的苄基酯，而没有引起消旋化。

  DOI：

  10.1246/bcsj.69.1099
• 作为产物：
  描述：

  4-(2-phenylacetoxy)benzyl (tert-butoxycarbonyl)seryl-L-isoleucinate 在 immobilized penicillin G acylase (300 U) 作用下， 以 甲醇 、 phosphate buffer 为溶剂， 反应 24.0h， 以80%的产率得到N-Boc-L-Ser-Ile-OH
  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

• Asymmetric Total Synthesis and Stereochemical Revision of Gymnangiamide
  作者：Hitoshi Tone、Marie Buchotte、Céline Mordant、Eric Guittet、Tahar Ayad、Virginie Ratovelomanana-Vidal

  DOI：10.1021/ol900184d

  日期：2009.5.7

  The asymmetric total synthesis of the originally proposed structure of gymnangiamide, a cytotoxic pentapeptide isolated from the marine hydroid Gymnangium regae Jaderholm, has been achieved. Key to the synthesis was the use of asymmetric hydrogenation of alpha-substituted, beta-ketoesters through dynamic kinetic resolution for the preparation of nonproteinogenic chiral amino acids. The disparity of the NMR spectra between the synthetic material containing the L-serine residue and the natural product required a revision of the proposed structure.
• 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.