(S)-pyroglutamyl-(S)-phenylalanine ethyl ester | 64154-98-9

• 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: (S)-pyroglutamyl-(S)-phenylalanine ethyl ester
• 英文别名: Glp-Phe-OMe；Glp-Phe-OCH3；L-Pyroglutamyl-L-phenylalanine Methyl Ester；methyl (2S)-2-[[(2S)-5-oxopyrrolidine-2-carbonyl]amino]-3-phenylpropanoate
• CAS: 64154-98-9
• 化学式: C₁₅H₁₈N₂O₄
• 分子量: 290.319
• InChiKey: YKGJSUNBVMJPQI-RYUDHWBXSA-N

物化性质

• 熔点：
  74 °C(Solv: ethyl ether (60-29-7))
• 沸点：
  577.1±50.0 °C(Predicted)
• 密度：
  1.233±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.4
• 重原子数：
  21
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.4
• 拓扑面积：
  84.5
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  L-丙氨酸4-硝基酰苯胺 、 (S)-pyroglutamyl-(S)-phenylalanine ethyl ester 在 α-chymotrypsin 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 11.0h， 以82%的产率得到Glp-Phe-Ala-pNA
  参考文献：
  名称：

  Selective chromogenic and fluorogenic peptide substrates for the assay of cysteine peptidases in complex mixtures

  摘要：

  This study describes the design, synthesis, and use of selective peptide substrates for cysteine peptidases of the Cl papain family, important in many biological processes. The structure of the newly synthesized substrates is Glp-Xaa-Ala-Y (where Glp = pyroglutamyl; Xaa = Phe or Val; and Y = pNA [p-nitroanilide], AMC [4-amino-7-methylcoumaride], or AFC [4-amino-7-trifluoromethyl-coumaridel]). Substrates were synthesized enzymatically to guarantee selectivity of the reaction and optical purity of the target compounds, simplifying the scheme of synthesis and isolation of products. The hydrolysis of the synthesized substrates was evaluated by C1 cysteine peptidases from different organisms and with different functions, including plant enzymes papain, bromelain, ficin, and mammalian lysosomal cathepsins B and L. The new substrates were selective for C1 cysteine peptidases and were not hydrolyzed by serine, aspartic, or metallo peptidases. We demonstrated an application of the selectivity of the synthesized substrates during the chromatographic separation of a multicomponent set of digestive peptidases from a beetle, Tenebrio molitor. Used in combination with the cysteine peptidase inhibitor E-64, these substrates were able to differentiate cysteine peptidases from peptidases of other classes in midgut extracts from T. molitor larvae and larvae of the genus Tribolium; thus, they are useful in the analysis of complex mixtures containing peptidases from different classes. Published by Elsevier Inc.

  DOI：

  10.1016/j.ab.2013.12.032
• 作为产物：
  描述：

  (S)-[2,2-双(三氟甲基)-5-氧代-1,3-恶唑烷-4-基]丙酸 在 氯化亚砜 、 N,N-二甲基甲酰胺 作用下， 以 乙醚 、 二氯甲烷 为溶剂， 反应 72.0h， 生成 (S)-pyroglutamyl-(S)-phenylalanine ethyl ester
  参考文献：
  名称：

  Hexafluoroacetone as Protecting and Activating Reagent: An Efficient Strategy for Activation of Pyroglutamic Acid and Homologues

  摘要：

  DOI：

  10.3987/com-03-s34

文献信息

• Acylated cyanamide compounds
  申请人：Regents of the University of Minnesota

  公开号：US04940816A1

  公开（公告）日：1990-07-10

  Acylated cyanamide compounds useful for ethanol deterrence of the formula RCONHCN, wherein R is a lipophilic acyl group or is derived from an (N-substituted)-alpha-aminoacyl group.

  以下是翻译结果： 酰化氰胺化合物对乙醇具有阻止作用，其化学式为RCONHCN，其中R为亲脂性酰基或由（N-取代）-α-氨基酰基基团衍生。
• Acylated cyanamide composition for treating ethanol ingestion
  申请人：Regents of the University of Minnesota

  公开号：US04726941A1

  公开（公告）日：1988-02-23

  Acylated cyanamide compounds useful for ethanol deterrence of the formula RCONHCN, wherein R is a lipophilic acyl group or is derived from an (N-substituted)-alpha-aminoacyl group.

  该化合物的化学式为RCONHCN，其中R为亲脂性酰基或来自（N-取代）-α-氨基酰基团，可用于乙醇防止。
• Acylated cyanamide composition
  申请人：Regents of the University of Minnesota

  公开号：US04870056A1

  公开（公告）日：1989-09-26

  Acylated cyanamide compounds useful for ethanol deterrence of the formula RCONHCN, wherein R is a lipophilic acyl group or is derived from an (N-substituted)-alpha-aminoacyl group.

  具有乙醇防止作用的酰化氰胺化合物的化学式为RCONHCN，其中R为亲脂性酰基或来自(N-取代)-α-氨基酰基基团。
• Chemoenzymatic synthesis of new fluorogenous substrates for cysteine proteases of the papain family
  作者：T. A. Semashko、E. N. Lysogorskaya、E. S. Oksenoit、A. V. Bacheva、I. Yu. Filippova

  DOI：10.1134/s1068162008030151

  日期：2008.5

  A chemoenzymatic synthesis was developed for new highly specific fluorogenic substrates for cysteine proteases of the papain family, Abz-Phe-Ala-pNA (I) and Glp-Phe-Ala-Amc (II) (Abz, pNA, Glp, and Amc are o-aminobenzoyl,p-nitroanilide, pyroglutamyl, and 4-amino-7-methylcoumaride, respectively). Substrate (I) was obtained in an aqueous-organic medium using native chymotrypsin. Substrate (II) was synthesized in DMF-MeCN by the treatment with chymotrypsin and subtilisin Carlsberg immobilized on polyvinyl alcohol cryogel. Hydrolysis of substrate (I) with papain, ficin, and bromelain was accompanied by a 15-fold increase in fluorescence intensity, and that of substrate (II), by a change in the fluorescence spectrum. Unambiguity of enzymatic hydrolysis of the substrates after the Ala residue was shown. The specific activity of the substrate hydrolysis with papain, bromelain, and ficin and was determined. Papain showed the greatest activity for both substrates. The activity of all proteases under study was essentially higher for substrate (II), than for substrate (I). The lowest detectable papain concentrations were 2.4 x 10(-10) M for (I) and 1.2 x 10(-11) M for (II). A high selectivity of cysteine proteases for Glp-Phe-Ala-Ame was established.
• NAGASAWA, HERBERT T.;KWON, CHUL-HOON
  作者：NAGASAWA, HERBERT T.、KWON, CHUL-HOON

  DOI：——

  日期：——