3-thiourea-L-phenylglycine

• 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: 3-thiourea-L-phenylglycine
• 英文别名: (2S)-2-amino-2-[3-(carbamothioylamino)phenyl]acetic acid
• 化学式: C₉H₁₁N₃O₂S
• 分子量: 225.271
• InChiKey: FIFOUTJIABHNTA-ZETCQYMHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.5
• 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：
  134
• 氢给体数：
  4
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  3-硝基苯乙烯 在 palladium on activated charcoal 2,6-二甲基吡啶 、 2,2,6,6-tetramethyl-piperidine-N-oxyl 、 sodium hypochlorite 、 四氧化锇 、 sodium dithionite 、 (DHQ)2-PHAL 、 次氯酸叔丁酯 、 氢气 、 三溴化硼 、 potassium carbonate 、 1,1'-dioctyl-4,4'-bipyridinium dibromide 、 calcium carbonate 、 potassium bromide 作用下， 以 吡啶 、 甲醇 、 丙醇 、 sodium hydroxide 、 二氯甲烷 、 水 、 丙酮 为溶剂， -78.0~35.0 ℃ 、413.68 kPa 条件下， 反应 22.0h， 生成 3-thiourea-L-phenylglycine
  参考文献：
  名称：

  Asymmetric Synthesis of Conformationally Restricted l-Arginine Analogues as Active Site Probes of Nitric Oxide Synthase

  摘要：

  Using the catalytic asymmetric Sharpless carbamate aminohydroxylation, conformationally restricted L-arginine and L-homoarginine derivatives (5-8) were prepared in good enantiomeric excess to investigate the binding requirements of L-arginine-based compounds with nitric oxide synthase. The L-arginine derivatives (5 and 6) inhibited both the inducible and neuronal isoforms of nitric oxide synthase with little isoform selectivity (5, IC50 = 42 and 144 mu M, 6, 8 and 12 mu M, respectively). The guanidine-containing compound (5) did not act as a nitric oxide producing substrate for nitric oxide synthase. The ability of these compounds to interact with the enzyme supports the idea that L-arginine-based inhibitors bind to the enzyme in a folded conformation. The L-homoarginine derivatives (7 and 8) did not interact with the enzyme as either substrates or inhibitors. The two-carbon L-arginine homologue (9), prepared from L-phenylalanine, demonstrated the greatest isoform selective inhibition of the compounds examined (IC50(iNOS) = 19 and IC50- (nNOS) = 147 mu M, IC50(nNOS)/IC(50)i(NOS) = 7.7). These results suggest isoform selective inhibition may be related to the folded conformations required for binding of these higher L-arginine homologues.

  DOI：

  10.1021/jo982161f