4-(decanoylamino)benzenesulfonamide | 5579-68-0

• 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-(decanoylamino)benzenesulfonamide
• 英文别名: N-decanoyl-sulfanilic acid amide；N-Decanoyl-sulfanilsaeure-amid；N-(4-sulfamoylphenyl)decanamide
• CAS: 5579-68-0
• 化学式: C₁₆H₂₆N₂O₃S
• 分子量: 326.46
• InChiKey: FAGSBFXBWGCSCA-UHFFFAOYSA-N

物化性质

• 密度：
  1.151±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.1
• 重原子数：
  22
• 可旋转键数：
  10
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  97.6
• 氢给体数：
  2
• 氢受体数：
  4

安全信息

• 海关编码：
  2935009090

反应信息

• 作为反应物：
  描述：

  4-(decanoylamino)benzenesulfonamide 在 4-二甲氨基吡啶 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三氟乙酸 作用下， 生成 {[6-(4-Decanoylamino-benzenesulfonylaminocarbonyl)-naphthalen-2-yl]-difluoro-methyl}-phosphonic acid
  参考文献：
  名称：

  Acylsulfonamide-containing PTP1B inhibitors designed to mimic an enzyme-bound water of hydration

  摘要：

  Previously, it had been reported that 6-(phosphonodifluoromethyl)-2-naphthoic acid binds to the protein-tyrosine phosphatase PTP1B with its 2-carboxyl group interacting only indirectly through a bridging water molecule. Reported herein is a family of new analogues that utilize acylsulfonamido functionality both to mimic this water of hydration and to provide an additional new site for elaboration not found in the parent carboxyl-containing analogue. Target acylsulfonamides were prepared in two steps from commercially available primary sulfonamides, which were selected based on in silico screening for their potential ability to interact with one of three binding surfaces proximal to the PTP1B catalytic site. In general, modest potency enhancements were observed. Arylacylsulfonamides represent a structure-based extension of inhibitor design that may have broader utility in the development of PTP1B inhibitors. (C) 2003 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(03)00635-8
• 作为产物：
  描述：

  N-苯基癸酰胺 在 1.) chlorosulfonation, 2.) amination 作用下， 生成 4-(decanoylamino)benzenesulfonamide
  参考文献：
  名称：

  Footprint Catalysis. II. Molecular Recognition of Footprint Catalytic Sites

  摘要：

  为了研究 "足印 "催化位点的分子识别能力，我们通过竞争抑制常数 Ki 估算了九种 "足印 "催化剂对十一种与模板分子密切相关的竞争性抑制剂的亲和力。对亲和力的研究表明，"足印 "催化位点的识别具有高度特异性，不仅能识别结合分子的整体结构，还能识别其部分结构。

  DOI：

  10.1246/bcsj.61.3999

文献信息

• Sulphonic acid amide compounds
  申请人：WINTHROP CHEM CO INC

  公开号：US02169971A1

  公开（公告）日：1939-08-15
• DE725537
  申请人：——

  公开号：——

  公开（公告）日：——
• Acylsulfonamide-containing PTP1B inhibitors designed to mimic an enzyme-bound water of hydration
  作者：Ding-Guo Liu、Yang Gao、Johannes H. Voigt、Kyeong Lee、Marc C. Nicklaus、Li Wu、Zhong-Yin Zhang、Terrence R. Burke

  DOI：10.1016/s0960-894x(03)00635-8

  日期：2003.9

  Previously, it had been reported that 6-(phosphonodifluoromethyl)-2-naphthoic acid binds to the protein-tyrosine phosphatase PTP1B with its 2-carboxyl group interacting only indirectly through a bridging water molecule. Reported herein is a family of new analogues that utilize acylsulfonamido functionality both to mimic this water of hydration and to provide an additional new site for elaboration not found in the parent carboxyl-containing analogue. Target acylsulfonamides were prepared in two steps from commercially available primary sulfonamides, which were selected based on in silico screening for their potential ability to interact with one of three binding surfaces proximal to the PTP1B catalytic site. In general, modest potency enhancements were observed. Arylacylsulfonamides represent a structure-based extension of inhibitor design that may have broader utility in the development of PTP1B inhibitors. (C) 2003 Elsevier Ltd. All rights reserved.
• Footprint Catalysis. II. Molecular Recognition of Footprint Catalytic Sites
  作者：Kensaku Morihara、Emiko Nishihata、Mari Kojima、Sayoko Miyake

  DOI：10.1246/bcsj.61.3999

  日期：1988.11

  In order to investigate the molecular recognition capability of “footprint” catalytic sites, the affinities of nine “footprint” catalysts for eleven competitive inhibitors, closely related to template molecules, were estimated through the competitive inhibition constants, Ki. An examination of the affinity revealed that the recognition by “footprint” catalytic sites was so highly specific that it could recognize not only the whole, but also the partial, structures of the bound molecules.

  为了研究 "足印 "催化位点的分子识别能力，我们通过竞争抑制常数 Ki 估算了九种 "足印 "催化剂对十一种与模板分子密切相关的竞争性抑制剂的亲和力。对亲和力的研究表明，"足印 "催化位点的识别具有高度特异性，不仅能识别结合分子的整体结构，还能识别其部分结构。