9,10-dioxa-syn-(carboxymethylthiomethyl, methyl)(methyl, methyl)-bimane | 119843-35-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡唑并吡唑类
• 英文名称: 9,10-dioxa-syn-(carboxymethylthiomethyl, methyl)(methyl, methyl)-bimane
• 英文别名: {[(2,5,6-Trimethyl-1,7-dioxo-1H,7H-pyrazolo[1,2-a]pyrazol-3-yl)methyl]sulfanyl}acetic acid；2-[(1,2,6-trimethyl-3,5-dioxopyrazolo[1,2-a]pyrazol-7-yl)methylsulfanyl]acetic acid
• CAS: 119843-35-5
• 化学式: C₁₂H₁₄N₂O₄S
• 分子量: 282.32
• InChiKey: QGILUUYBCLGCBT-UHFFFAOYSA-N

物化性质

• 沸点：
  445.6±55.0 °C(Predicted)
• 密度：
  1.47±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.9
• 重原子数：
  19
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  103
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  9,10-dioxa-syn-(carboxymethylthiomethyl, methyl)(methyl, methyl)-bimane 在 盐酸 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 、 三乙胺 作用下， 以 1,4-二氧六环 、 N,N-二甲基甲酰胺 为溶剂， 反应 2.0h， 生成 S-[9,10-dioxa-syn-(methyl,methyl)(methylene,methyl)-bimane]-thioglycolyl-glycine
  参考文献：
  名称：

  New fluorogenic substrates for microdetermination of carboxypeptidase A.

  摘要：

  作为对羧肽酶A活性敏感荧光测定法开发的一部分，制备了含有色氨酸的双苯乙烯肽，即S-[9, 10-二氧-反-(甲基, 甲基).-(亚甲基, 甲基)-双苯乙烯]-硫代乙酸-(甘氨酸)-L-色氨酸和O-{S-[9, 10-二氧-反-(甲基, 甲基)(亚甲基, 甲基)-双苯乙烯]-硫代乙酸}-DL-3-吲哚乳酸，并显示出它们是微量测定羧肽酶A活性的良好荧光底物。

  DOI：

  10.1248/cpb.36.4494
• 作为产物：
  描述：

  荧光专用试剂 、 巯基乙酸 在 三乙胺 作用下， 以 乙腈 为溶剂， 以52%的产率得到9,10-dioxa-syn-(carboxymethylthiomethyl, methyl)(methyl, methyl)-bimane
  参考文献：
  名称：

  New fluorogenic substrates for microdetermination of carboxypeptidase A.

  摘要：

  作为对羧肽酶A活性敏感荧光测定法开发的一部分，制备了含有色氨酸的双苯乙烯肽，即S-[9, 10-二氧-反-(甲基, 甲基).-(亚甲基, 甲基)-双苯乙烯]-硫代乙酸-(甘氨酸)-L-色氨酸和O-{S-[9, 10-二氧-反-(甲基, 甲基)(亚甲基, 甲基)-双苯乙烯]-硫代乙酸}-DL-3-吲哚乳酸，并显示出它们是微量测定羧肽酶A活性的良好荧光底物。

  DOI：

  10.1248/cpb.36.4494

文献信息

• Chemoenzymatic Synthesis of N-<i>Ras</i> Lipopeptides
  作者：Edgar Nägele、Michael Schelhaas、Norman Kuder、Herbert Waldmann

  DOI：10.1021/ja9805627

  日期：1998.7.1

  For the study of biological phenomena influenced by the plasma-membrane-bound Ras proteins and other lipidated proteins, characteristic peptides which embody the correct lipid modifications of their parent proteins (palmitoyl thioesters and farnesyl thioethers), as well as analogues thereof, may serve as suitable tools. For the construction of such acid- and base-labile peptide conjugates, the enzyme-labile p-acetoxybenzyloxycarbonyl (AcOZ) urethane blocking group was developed. The acetate moiety within the AcOZ group is easily saponified by treatment with acetyl esterase or lipase. After cleavage of the acetate group the resulting quinone methide spontaneously fragments, resulting in the liberation of the desired peptide or peptide conjugates. This enzymatic protecting group technique formed the key step in the synthesis of the characteristic S-palmitoylated and S-farnesylated C-terminus of the human N-Ras protein. Deprotections are so mild that no undesired side reactions of the lipid conjugates are observed (i.e., no hydrolysis or beta-elimination of the thioester and no acid-mediated attack on the double bonds of the farnesyl group). The combination of enzymatic protecting group techniques with classical chemical methods allowed access to various fluorescent-labeled and differently lipid-modified Rns lipopeptides. Their application in biological experiments enabeled the study of the structural requirements for the acylation of Ras sequence motifs in vivo and gave insight into the subcellular site at which these modifications occur. The results indicate that the plasma membrane is a major site of cellular S-acylation. This supports a mechanism for the selective subcellular localization of lipidated proteins, including the Rns proteins themselves, by kinetic targeting to the plasma membrane.
• BAEYENS, WILLY R. G.;VAN, DER WEKEN GUIDO;DE, MOERLOOSE PROSPER, ANAL. CHIM. ACTA, 205,(1988) N 1-2, 43-51
  作者：BAEYENS, WILLY R. G.、VAN, DER WEKEN GUIDO、DE, MOERLOOSE PROSPER

  DOI：——

  日期：——
• Chemoenzymatic Synthesis of Fluorescent N-Ras Lipopeptides and Their Use in Membrane Localization Studies in Vivo
  作者：Herbert Waldmann、Michael Schelhaas、Edgar Nägele、Jürgen Kuhlmann、Alfred Wittinghofer、Hans Schroeder、John R. Silvius

  DOI：10.1002/anie.199722381

  日期：1997.11.3
• New fluorogenic substrates for microdetermination of carboxypeptidase A.
  作者：EISUKE SATO、YUICHI KANAOKA

  DOI：10.1248/cpb.36.4494

  日期：——

  As a part of the development of a sensitive fluorometric assay for the activity of carboxypeptidase A, bimane-peptides containing tryptophan, i.e., S-[9, 10-dioxa-syn-(methyl, methyl).-(methylene, methyl)-bimane]-thioglycoly1-(glycyl)-L-tryptophan and O-S-[9, 10-dioxa-syn-(methyl, methyl)(methylene, methyl)-bimane]-thioglycolyl}-DL-3-indolelactic acid, were prepared and shown be good fluorogenic substrates for microdetermination of carboxypeptidase A activity.

  作为对羧肽酶A活性敏感荧光测定法开发的一部分，制备了含有色氨酸的双苯乙烯肽，即S-[9, 10-二氧-反-(甲基, 甲基).-(亚甲基, 甲基)-双苯乙烯]-硫代乙酸-(甘氨酸)-L-色氨酸和O-S-[9, 10-二氧-反-(甲基, 甲基)(亚甲基, 甲基)-双苯乙烯]-硫代乙酸}-DL-3-吲哚乳酸，并显示出它们是微量测定羧肽酶A活性的良好荧光底物。