5-Azidopentane-1-thiol | 1610532-46-1

• 分子结构分类: 有机化合物 - 有机1,3-偶极化合物 - 烯丙基型1,3-偶极有机化合物
• 英文名称: 5-Azidopentane-1-thiol
• 英文别名: 5-azidopentane-1-thiol
• CAS: 1610532-46-1
• 化学式: C₅H₁₁N₃S
• 分子量: 145.228
• InChiKey: RIFHIVVYIJWCAG-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  9
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  15.4
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  5-Azidopentane-1-thiol 在 氨 、 potassium carbonate 、 copper(II) sulfate 、 sodium ascorbate 作用下， 以 四氢呋喃 、 甲醇 、 水 、 丙酮 为溶剂， 反应 32.0h， 生成 2-[[1-[5-[(2-acetamido-β-D-glucopyranosyl)thio]pentyl]-1H-1,2,3-triazol-4-yl]methyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
  参考文献：
  名称：

  Selective inhibition of β-N-acetylhexosaminidases by thioglycosyl–naphthalimide hybrid molecules

  摘要：

  To develop selective inhibitors for beta-N-acetylhexosaminidases which are involved in a myriad of physiological processes, a series of novel thioglycosyl-naphthalimide hybrid inhibitors were designed, synthesized and evaluated for inhibition activity against glycosyl hydrolase family 20 and 84 (GH20 and GH84) beta-N-acetylhexosaminidases. These compounds which incorporate groups with varied sizes and lengths at the linker region between thioglycosyl moiety and naphthalimide moiety are designed to improve the selectivity and stacking interactions. The GH84 human O-GlcNAcase (hOGA) was sensitive to the subtle changes in the linker region and the optimal choice is a small size linker with six atoms length. And the GH20 insect beta-N-acetylhexosaminidase OfHex1 could tolerate compounds with a hydrophobic bulky linker. Especially, the compound 5c (hOGA, K-i = 3.46 mu M; OfHex1, K-i > 200 mu M) and the compound 6f (hOGA, K-i > 200 mu M; OfHex1, K-i = 21.81 mu M) displayed high selectivity. The molecular docking results indicated that the inhibition mechanism was different between the two families due to their different structural characteristics beyond the active sites. These results provide some promising clues to improve selectivity of potent molecules against beta-N-acetylhexosaminidases. (C) 2017 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2017.11.042
• 作为产物：
  描述：

  1-azido-5-bromopentane 在 硫脲 、 sodium hydroxide 、 硫酸 作用下， 以 乙醇 为溶剂， 反应 16.41h， 生成 5-Azidopentane-1-thiol
  参考文献：
  名称：

  Reactions in Elastomeric Nanoreactors Reveal the Role of Force on the Kinetics of the Huisgen Reaction on Surfaces

  摘要：

  The force dependence of the copper-free Huisgen cycloaddition between an alkyne and a surface-bound azide was examined in elastomeric nanoreactors. These studies revealed that pressure and chain length are critical factors that determine the reaction rate. These experiments demonstrate the central role of pressure and surface structure on interfacial processes that are increasingly important in biology, materials science, and nanotechnology.

  DOI：

  10.1021/ja504137u

文献信息

• Design, Synthesis and Evaluation of Triazole-Pyrimidine Analogues as SecA Inhibitors
  作者：Jianmei Cui、Jinshan Jin、Arpana Sagwal Chaudhary、Ying-hsin Hsieh、Hao Zhang、Chaofeng Dai、Krishna Damera、Weixuan Chen、Phang C. Tai、Binghe Wang

  DOI：10.1002/cmdc.201500447

  日期：2016.1

  SecA, a key component of the bacterial Sec‐dependent secretion pathway, is an attractive target for the development of new antimicrobial agents. Through a combination of virtual screening and experimental exploration of the surrounding chemical space, we identified a hit bistriazole SecA inhibitor, SCA‐21, and studied a series of analogues by systematic dissections of the core scaffold. Evaluation

  SecA 是细菌 Sec 依赖性分泌途径的关键组成部分，是开发新型抗菌药物的一个有吸引力的靶点。通过虚拟筛选和对周围化学空间的实验探索相结合，我们鉴定了一种热门的双三唑 SecA 抑制剂 SCA-21，并通过对核心支架的系统解剖研究了一系列类似物。对这些类似物的评估使我们能够在 SecA 抑制中建立初步的结构-活性关系。该组中最好的化合物是低至亚微摩尔浓度的 SecA 依赖性蛋白质传导通道活性和蛋白质易位活性的有效抑制剂。它们还具有针对各种细菌菌株的最小抑菌浓度 (MIC) 值，与 SecA 和蛋白质易位抑制数据密切相关。这些化合物可有效对抗具有不同水平外排泵活性的耐甲氧西林金黄色葡萄球菌菌株，表明 SecA 抑制剂具有消除多药耐药性影响的能力。药物亲和力响应靶点稳定性和蛋白质下拉测定的研究结果与 SecA 作为这些化合物的靶点一致。
• Reactions in Elastomeric Nanoreactors Reveal the Role of Force on the Kinetics of the Huisgen Reaction on Surfaces
  作者：Xu Han、Shudan Bian、Yong Liang、K. N. Houk、Adam B. Braunschweig

  DOI：10.1021/ja504137u

  日期：2014.7.30

  The force dependence of the copper-free Huisgen cycloaddition between an alkyne and a surface-bound azide was examined in elastomeric nanoreactors. These studies revealed that pressure and chain length are critical factors that determine the reaction rate. These experiments demonstrate the central role of pressure and surface structure on interfacial processes that are increasingly important in biology, materials science, and nanotechnology.
• Selective inhibition of β-N-acetylhexosaminidases by thioglycosyl–naphthalimide hybrid molecules
  作者：Wei Chen、Shengqiang Shen、Lili Dong、Jianjun Zhang、Qing Yang

  DOI：10.1016/j.bmc.2017.11.042

  日期：2018.1

  To develop selective inhibitors for beta-N-acetylhexosaminidases which are involved in a myriad of physiological processes, a series of novel thioglycosyl-naphthalimide hybrid inhibitors were designed, synthesized and evaluated for inhibition activity against glycosyl hydrolase family 20 and 84 (GH20 and GH84) beta-N-acetylhexosaminidases. These compounds which incorporate groups with varied sizes and lengths at the linker region between thioglycosyl moiety and naphthalimide moiety are designed to improve the selectivity and stacking interactions. The GH84 human O-GlcNAcase (hOGA) was sensitive to the subtle changes in the linker region and the optimal choice is a small size linker with six atoms length. And the GH20 insect beta-N-acetylhexosaminidase OfHex1 could tolerate compounds with a hydrophobic bulky linker. Especially, the compound 5c (hOGA, K-i = 3.46 mu M; OfHex1, K-i > 200 mu M) and the compound 6f (hOGA, K-i > 200 mu M; OfHex1, K-i = 21.81 mu M) displayed high selectivity. The molecular docking results indicated that the inhibition mechanism was different between the two families due to their different structural characteristics beyond the active sites. These results provide some promising clues to improve selectivity of potent molecules against beta-N-acetylhexosaminidases. (C) 2017 Elsevier Ltd. All rights reserved.