methyl 2-(R,S)-2-(tert-butoxycarbonylamino)-4-mercaptobutanoate | 1043521-51-2

• 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: methyl 2-(R,S)-2-(tert-butoxycarbonylamino)-4-mercaptobutanoate
• 英文别名: methyl (tert-butoxycarbonyl)homocysteinate；methyl 2-[(tert-butoxycarbonyl)amino]-4-sulfanylbutanoate；N-Boc-DL-homocysteine methyl ester；Methyl 2-[(2-methylpropan-2-yl)oxycarbonylamino]-4-sulfanylbutanoate；methyl 2-[(2-methylpropan-2-yl)oxycarbonylamino]-4-sulfanylbutanoate
• CAS: 1043521-51-2
• 化学式: C₁₀H₁₉NO₄S
• 分子量: 249.331
• InChiKey: MAVQFIBKMPVZMF-UHFFFAOYSA-N

物化性质

• 沸点：
  360.8±37.0 °C(Predicted)
• 密度：
  1.113±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  16
• 可旋转键数：
  7
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  65.6
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  methyl 2-(R,S)-2-(tert-butoxycarbonylamino)-4-mercaptobutanoate 在 Hoveyda-Grubbs catalyst second generation potassium carbonate 作用下， 以 水 、 N,N-二甲基甲酰胺 、 叔丁醇 为溶剂， 反应 5.5h， 生成 BocAhcOMe
  参考文献：
  名称：

  OLEFIN METATHESIS REACTIONS OF AMINO ACIDS, PEPTIDES AND PROTEINS CONTAINING ALLYL SULFIDE GROUPS

  摘要：

  揭示了一种用于修饰氨基酸、蛋白质或肽的方法。该方法包括在促进烯烃交换反应的催化剂存在下，将含有碳-碳双键的化合物与含有烯丙基硫醚基团的氨基酸、蛋白质或肽反应，以形成修饰后的氨基酸、蛋白质或肽。首选的碳-碳双键含有化合物包括碳水化合物。

  公开号：

  US20120178913A1
• 作为产物：
  描述：

  methyl 2-amino-4-{[3-amino-4-methoxy-4-oxobutyl]disuIfanyl}butanoate 在 sodium acetate 、 溶剂黄146 、 三乙胺 、 三苯基膦 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 2.0h， 生成 methyl 2-(R,S)-2-(tert-butoxycarbonylamino)-4-mercaptobutanoate
  参考文献：
  名称：

  未修饰肽与 5-18F-(三氟甲基)二苯并噻吩三氟甲磺酸盐的 18F-三氟甲基化

  摘要：

  5-(三氟甲基)-二苯并噻吩三氟甲磺酸盐的 18F 标记，通常称为 Umemoto 试剂，已通过卤素交换 18F-氟化与 18F-氟化物，然后与 Oxone 和三氟甲磺酸酐氧化环化来完成。这种新的 18F 试剂允许在硫醇半胱氨酸残基处对未修饰的肽进行直接化学选择性 18F 标记。

  DOI：

  10.1021/jacs.7b10227

文献信息

• The development of a new class of inhibitors for betaine-homocysteine S-methyltransferase
  作者：Jan Pícha、Václav Vaněk、Miloš Buděšínský、Jana Mládková、Timothy A. Garrow、Jiří Jiráček

  DOI：10.1016/j.ejmech.2013.04.039

  日期：2013.7

  Betaine-homocysteine S-methyltransferase (BHMT) is an important zinc-dependent methyltransferase that uses betaine as the methyl donor for the remethylation of homocysteine to form methionine. In the liver, BHMT performs to half of the homocysteine remethylation. In this study, we systematically investigated the tolerance of the enzyme for modifications at the "homocysteine" part of the previously reported potent inhibitor (R,S)-5-(3-amino-3-carboxy-propylsulfanyl)-pentanoic acid (1). In the new compounds, which are S-alkylated homocysteine derivatives, we replaced the carboxylic group in the "homocysteine" part of inhibitor 1 with different isosteric moieties (tetrazole and oxadiazolone); we suppressed the carboxylic negative charge by amidations; we enhanced acidity by replacing the carboxylate with phosphonic or phosphinic acids; and we introduced pyrrolidine steric constraints. Some of these compounds display high affinity toward human BHMT and may be useful for further pharmacological studies of this enzyme. Although none of the new compounds were more potent inhibitors than the reference inhibitor 1, this study helped to completely define the structural requirements of the active site of BHMT and revealed the remarkable selectivity of the enzyme for homocysteine. (C) 2013 Elsevier Masson SAS. All rights reserved.
• Allyl Sulfides Are Privileged Substrates in Aqueous Cross-Metathesis: Application to Site-Selective Protein Modification
  作者：Yuya A. Lin、Justin M. Chalker、Nicola Floyd、Gonçalo J. L. Bernardes、Benjamin G. Davis

  DOI：10.1021/ja8026168

  日期：2008.7.1

  Allyl sulfides undergo efficient cross-metathesis in aqueous media with Hoveyda-Grubbs second generation catalyst 1. The high reactivity of allyl sulfides in cross-metathesis was exploited in the first examples of cross-metathesis on a protein surface. S-Allylcysteine was incorporated chemically into the protein, providing the requisite allyl sulfide handle. Preliminary efforts to genetically incorporate S-allylcysteine into proteins are also reported.
• SAR around (l)-S-adenosyl-l-homocysteine, an inhibitor of human DNA methyltransferase (DNMT) enzymes
  作者：Oscar M. Saavedra、Ljubomir Isakovic、David B. Llewellyn、Lijie Zhan、Naomy Bernstein、Stephen Claridge、Franck Raeppel、Arkadii Vaisburg、Nadine Elowe、Andrea J. Petschner、Jubrail Rahil、Norman Beaulieu、A. Robert MacLeod、Daniel Delorme、Jeffrey M. Besterman、Amal Wahhab

  DOI：10.1016/j.bmcl.2009.03.113

  日期：2009.5

  The inhibitory activity of base-modified SAH analogues and the specificity of inhibiting human DNMT1 and DNMT3b2 enzymes was explored. The 6-amino group was essential while the 7-N of the adenine ring of SAH could be replaced by CH- without loss of activity against both enzymes. The introduction of small groups at the 2-position of the adenine moiety favors DNMT1 over DNMT3b2 inhibition whereas alkylation of the N-6-amino moiety favors the inhibition of DNMT3b2 enzyme. (C) 2009 Elsevier Ltd. All rights reserved.
• ¹⁸F-Trifluoromethylation of Unmodified Peptides with 5-¹⁸F-(Trifluoromethyl)dibenzothiophenium Trifluoromethanesulfonate
  作者：Stefan Verhoog、Choon Wee Kee、Yanlan Wang、Tanatorn Khotavivattana、Thomas C. Wilson、Veerle Kersemans、Sean Smart、Matthew Tredwell、Benjamin G. Davis、Véronique Gouverneur

  DOI：10.1021/jacs.7b10227

  日期：2018.2.7

  18F-labeling of 5-(trifluoromethyl)-dibenzothiophenium trifluoromethanesulfonate, commonly referred to as the Umemoto reagent, has been accomplished applying a halogen exchange 18F-fluorination with 18F-fluoride, followed by oxidative cyclization with Oxone and trifluoromethanesulfonic anhydride. This new 18F-reagent allows for the direct chemoselective 18F-labeling of unmodified peptides at the thiol cysteine

  5-(三氟甲基)-二苯并噻吩三氟甲磺酸盐的 18F 标记，通常称为 Umemoto 试剂，已通过卤素交换 18F-氟化与 18F-氟化物，然后与 Oxone 和三氟甲磺酸酐氧化环化来完成。这种新的 18F 试剂允许在硫醇半胱氨酸残基处对未修饰的肽进行直接化学选择性 18F 标记。
• OLEFIN METATHESIS REACTIONS OF AMINO ACIDS, PEPTIDES AND PROTEINS CONTAINING ALLYL SULFIDE GROUPS
  申请人：Lin Yuya Angel

  公开号：US20120178913A1

  公开（公告）日：2012-07-12

  A method for the modification of an amino acid, protein or peptide is disclosed. The method comprises reacting a carbon-carbon double bond-containing compound with an amino acid, a protein or a peptide containing an allyl sulfide group in the presence of a catalyst which promotes olefin metathesis, to form a modified amino acid, protein or peptide. Preferred carbon-carbon double bond-containing compounds include carbohydrates.

  揭示了一种用于修饰氨基酸、蛋白质或肽的方法。该方法包括在促进烯烃交换反应的催化剂存在下，将含有碳-碳双键的化合物与含有烯丙基硫醚基团的氨基酸、蛋白质或肽反应，以形成修饰后的氨基酸、蛋白质或肽。首选的碳-碳双键含有化合物包括碳水化合物。