4-(2,2-dichloroacetamido)benzoic acid | 7146-73-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 4-(2,2-dichloroacetamido)benzoic acid
• 英文别名: Dichloroacetyl-p-aminobenzoic acid；4-(2,2-dichloro-acetylamino)-benzoic acid；4-(2,2-Dichlor-acetylamino)-benzoesaeure；p-Dichloracetyl-amino-benzoesaeure；4-Dichloracetamino-benzoesaeure；4-[(Dichloroacetyl)amino]benzoic acid；4-[(2,2-dichloroacetyl)amino]benzoic acid
• CAS: 7146-73-8
• 化学式: C₉H₇Cl₂NO₃
• 分子量: 248.065
• InChiKey: FELCOLZFVJIGLE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  15
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  66.4
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  甲醇 、 4-(2,2-dichloroacetamido)benzoic acid 在 三氟化硼 作用下， 生成 Dichloroacetyl-p-aminobenzoic acid methyl ester
  参考文献：
  名称：

  Generation of Antibodies to Di- and Trichloroacetylated Proteins and Immunochemical Detection of Protein Adducts in Rats Treated with Perchloroethene

  摘要：

  Antibodies directed against chemical specific protein modifications are valuable tools to detect and comparatively quantify protein modifications. Both N-epsilon-(dichloroacetyl)-L-lysine and N-epsilon-(trichloroacety)l-L-lysine have been detected as modified amino acids in liver and kidneys of rats treated with perchloroethene (PER) after proteolysis. These protein modifications are formed by the interaction of reactive metabolites formed from PER with proteins. In this study we developed monospecific antibodies to dichloroacetylated and to trichloroacetylated amino acids to detect modified proteins in the target organs of PER toxicity. These antibodies were prepared by immunization of rabbits with modified keyhole limpet hemocyanin (KLH) coupled with either the dichloroacetyl or trichloroacetyl moiety. Enzyme-linked immunosorbent assays (ELISA) indicated that the polyclonal rabbit sera recognized dichloroacetylated or trichloroacetylated rabbit serum albumin (RSA), but not unmodified protein. Therefore, we further purified rabbit antisera on either N-epsilon-(dichloroacetyl)-L-lysine or N-epsilon-(trichloroacetyl)-L-lysine immobilized to immunoaffinity columns to obtain monospecific antibodies. The potential of these antibodies in the detection of di- and trichloroacetylated proteins and their selectivity for the desired dichloroacetyl or trichloroacetyl group was demonstrated in competitive enzme-linked immunosorbent assays with several structurally related compounds. Anti-dichloroacetyl (anti-DCA) antibody binding to dichloroacetylated RSA was inhibited by N-epsilon-(dichloroacetyl)L-lysine with an IC50 value of 150 mu M whereas inhibition by N-epsilon-(monochloroacetyl)-L-lysine and N-epsilon-(trichloroacetyl)-L-lysine showed an IC50 value of 100 mM. The binding of the antitrichloroacetyl (anti-TCA) antibody to trichloroacetylated RSA was inhibited by N-epsilon-(dichloroacetyl)-L-lysine with an IC50 value of 80 mM. The inhibition by N-epsilon-(trichloroacetyl)-L-lysine was again 3 orders of magnitude stronger resulting in an IC50 value of 90 mu M. N-epsilon-(acetyl)-L-lysine and unmodified RSA did not effect antibody binding to the chemically modified antigen. The antibodies were also successfully applied to detect modified proteins in subcellular fractions of liver and kidney from PER treated rats demonstrated in immunoblot. Protein adduct formation from different PER metabolism pathways was confirmed by the observation that the majority of dichloroacetylated proteins were located in kidney mitochondria and trichloroacetylated proteins were located in liver microsomes.

  DOI：

  10.1021/tx9800102
• 作为产物：
  描述：

  二氯乙酰氯 、 对氨基苯甲酸 生成 4-(2,2-dichloroacetamido)benzoic acid
  参考文献：
  名称：

  Potential Antivirals. I. Simple Analogs of Chloramphenicol (Chloromycetin)

  摘要：

  DOI：

  10.1021/ja01143a524

文献信息

• Dichloromeldrum’s Acid (DiCMA): A Practical and Green Amine Dichloroacetylation Reagent
  作者：David M. Heard、Alastair J. J. Lennox

  DOI：10.1021/acs.orglett.1c00850

  日期：2021.5.7

  dichloroacetylation of anilines and alkyl amines to produce α,α-dichloroacetamides, which are important motifs for medicinal chemistry. Products are formed in good to excellent yields with reagent grade solvents, and, as the only byproducts are acetone and CO2, no column chromatography is required. Thus, this reagent is practical, efficient, and green for the dichloroacetylation of primary amines.

  引入二氯甲mel酸是一种稳定的，不挥发的试剂，用于苯胺和烷基胺的二氯乙酰化，以生产α，α-二氯乙酰胺，这是药物化学的重要主题。使用试剂级溶剂可形成高至极佳收率的产物，并且由于唯一的副产物是丙酮和CO 2，因此无需柱色谱法。因此，该试剂对于伯胺的二氯乙酰化是实用，有效和绿色的。
• Potential Antivirals. I. Simple Analogs of Chloramphenicol (Chloromycetin)
  作者：Arthur P. Phillips

  DOI：10.1021/ja01143a524

  日期：1952.12
• MIGAJCHUK I. V.; XASKIN I. G., ZH. PRIKL. XIMII, 1979, 52, HO 4, 946-947
  作者：MIGAJCHUK I. V.、 XASKIN I. G.

  DOI：——

  日期：——
• [EN] PIPERAZINE DERIVATIVES USEFUL AS HYPOGLYCEMIC AGENTS<br/>[FR] DERIVES DE PIPERAZINE POUVANT ETRE UTILISES COMME AGENTS HYPOGLYCEMIQUES
  申请人：SHAMAN PHARMACEUTICALS, INC.

  公开号：WO1999031096A1

  公开（公告）日：1999-06-24

  (EN) Piperazine derivatives useful as antihyperglycemic agents, pharmaceutical compositions comprising the piperazine derivatives and methods for their use are described. The piperazine derivatives are useful for the treatment of insulin-dependent diabetes mellitus (IDDM or Type I) and non-insulin dependent diabetes mellitus (NIDDM or Type II).(FR) L'invention concerne des dérivés de pipérazine présentant une grande utilité comme agents antihyperglycémiques. L'invention traite également de compositions pharmaceutiques comprenant des dérivés de pipérazine et des procédés d'utilisation de ces derniers. Les dérivés de pipérazine permettent de traiter le diabète sucré insulinodépendant (ou de type I) et le diabète sucré non insulinodépendant (ou de type II).
• Generation of Antibodies to Di- and Trichloroacetylated Proteins and Immunochemical Detection of Protein Adducts in Rats Treated with Perchloroethene
  作者：Axel Pähler、Gerhard Birner、Jean Parker、Wolfgang Dekant

  DOI：10.1021/tx9800102

  日期：1998.9.1

  Antibodies directed against chemical specific protein modifications are valuable tools to detect and comparatively quantify protein modifications. Both N-epsilon-(dichloroacetyl)-L-lysine and N-epsilon-(trichloroacety)l-L-lysine have been detected as modified amino acids in liver and kidneys of rats treated with perchloroethene (PER) after proteolysis. These protein modifications are formed by the interaction of reactive metabolites formed from PER with proteins. In this study we developed monospecific antibodies to dichloroacetylated and to trichloroacetylated amino acids to detect modified proteins in the target organs of PER toxicity. These antibodies were prepared by immunization of rabbits with modified keyhole limpet hemocyanin (KLH) coupled with either the dichloroacetyl or trichloroacetyl moiety. Enzyme-linked immunosorbent assays (ELISA) indicated that the polyclonal rabbit sera recognized dichloroacetylated or trichloroacetylated rabbit serum albumin (RSA), but not unmodified protein. Therefore, we further purified rabbit antisera on either N-epsilon-(dichloroacetyl)-L-lysine or N-epsilon-(trichloroacetyl)-L-lysine immobilized to immunoaffinity columns to obtain monospecific antibodies. The potential of these antibodies in the detection of di- and trichloroacetylated proteins and their selectivity for the desired dichloroacetyl or trichloroacetyl group was demonstrated in competitive enzme-linked immunosorbent assays with several structurally related compounds. Anti-dichloroacetyl (anti-DCA) antibody binding to dichloroacetylated RSA was inhibited by N-epsilon-(dichloroacetyl)L-lysine with an IC50 value of 150 mu M whereas inhibition by N-epsilon-(monochloroacetyl)-L-lysine and N-epsilon-(trichloroacetyl)-L-lysine showed an IC50 value of 100 mM. The binding of the antitrichloroacetyl (anti-TCA) antibody to trichloroacetylated RSA was inhibited by N-epsilon-(dichloroacetyl)-L-lysine with an IC50 value of 80 mM. The inhibition by N-epsilon-(trichloroacetyl)-L-lysine was again 3 orders of magnitude stronger resulting in an IC50 value of 90 mu M. N-epsilon-(acetyl)-L-lysine and unmodified RSA did not effect antibody binding to the chemically modified antigen. The antibodies were also successfully applied to detect modified proteins in subcellular fractions of liver and kidney from PER treated rats demonstrated in immunoblot. Protein adduct formation from different PER metabolism pathways was confirmed by the observation that the majority of dichloroacetylated proteins were located in kidney mitochondria and trichloroacetylated proteins were located in liver microsomes.