(4-chlorosulfonylnaphthalen-1-yl)carbamic acid benzyl ester | 848641-12-3

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: (4-chlorosulfonylnaphthalen-1-yl)carbamic acid benzyl ester
• 英文别名: benzyl N-(4-chlorosulfonylnaphthalen-1-yl)carbamate
• CAS: 848641-12-3
• 化学式: C₁₈H₁₄ClNO₄S
• 分子量: 375.832
• InChiKey: YMYQRXBBLRNNBU-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.3
• 重原子数：
  25
• 可旋转键数：
  5
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.06
• 拓扑面积：
  80.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (4-chlorosulfonylnaphthalen-1-yl)carbamic acid benzyl ester 、 2-amino-3-[4-(5-dimethylaminonaphthalene-1-sulfonyloxy)phenyl]propionic acid 在 sodium hydroxide 、 碳酸氢钠 作用下， 以 丙酮 为溶剂， 以2%的产率得到(S)-2-(4-Benzyloxycarbonylamino-naphthalene-1-sulfonylamino)-3-[4-(5-dimethylamino-naphthalene-1-sulfonyloxy)-phenyl]-propionic acid
  参考文献：
  名称：

  Improving Specificity vs Bacterial Thymidylate Synthases through N-Dansyl Modulation of Didansyltyrosine

  摘要：

  N,O-Didansyl-L-tyrosine (DDT) represented the starting lead for further development of novel non-substrate-like inhibitors of bacterial thymidylate synthase. The N-dansyl structure modulation led to a submicromolar inhibitor of Lactobacillus casei TS (LcTS), which is highly specific with respect to human TS (hTS). Using molecular dynamics simulation, a binding mode for DDT vs LcTS was predicted, explaining activity and species-specificity along the series.

  DOI：

  10.1021/jm0491445
• 作为产物：
  描述：

  1-Naphthalenesulfonicacid,4-amino-,diazotized,coupledwithDyer鈥檚mulberryextract 在 sodium hydroxide 、 五氯化磷 、 碳酸氢钠 作用下， 以 四氯化碳 、 N,N-二甲基甲酰胺 为溶剂， 生成 (4-chlorosulfonylnaphthalen-1-yl)carbamic acid benzyl ester
  参考文献：
  名称：

  Improving Specificity vs Bacterial Thymidylate Synthases through N-Dansyl Modulation of Didansyltyrosine

  摘要：

  N,O-Didansyl-L-tyrosine (DDT) represented the starting lead for further development of novel non-substrate-like inhibitors of bacterial thymidylate synthase. The N-dansyl structure modulation led to a submicromolar inhibitor of Lactobacillus casei TS (LcTS), which is highly specific with respect to human TS (hTS). Using molecular dynamics simulation, a binding mode for DDT vs LcTS was predicted, explaining activity and species-specificity along the series.

  DOI：

  10.1021/jm0491445

文献信息

• Improving Specificity vs Bacterial Thymidylate Synthases through <i>N</i>-Dansyl Modulation of Didansyltyrosine
  作者：Donatella Tondi、Alberto Venturelli、Stefania Ferrari、Stefano Ghelli、M. Paola Costi

  DOI：10.1021/jm0491445

  日期：2005.2.1

  N,O-Didansyl-L-tyrosine (DDT) represented the starting lead for further development of novel non-substrate-like inhibitors of bacterial thymidylate synthase. The N-dansyl structure modulation led to a submicromolar inhibitor of Lactobacillus casei TS (LcTS), which is highly specific with respect to human TS (hTS). Using molecular dynamics simulation, a binding mode for DDT vs LcTS was predicted, explaining activity and species-specificity along the series.