Ser-Ser-Trp | 1415888-19-5

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: Ser-Ser-Trp
• 英文别名: (2S)-2-[[(2S)-2-[[(2S)-2-amino-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-indol-3-yl)propanoic acid
• CAS: 1415888-19-5
• 化学式: C₁₇H₂₂N₄O₆
• 分子量: 378.385
• InChiKey: DKGRNFUXVTYRAS-UBHSHLNASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.6
• 重原子数：
  27
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  178
• 氢给体数：
  7
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  Ser-Ser-Trp 、 7-methoxycarbonylpterin 在 1,8-二氮杂双环[5.4.0]十一碳-7-烯 作用下， 以 甲醇 为溶剂， 以36%的产率得到(2S)-2-[[(2S)-2-[[(2S)-2-[(2-amino-4-oxo-3H-pteridine-7-carbonyl)amino]-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-indol-3-yl)propanoic acid
  参考文献：
  名称：

  Peptide-Conjugated Pterins as Inhibitors of Ricin Toxin A

  摘要：

  Several 7-peptide-substituted pterins were synthesized and tested as competitive active-site inhibitors of ricin toxin A (RTA). Focus began on dipeptide conjugates, and these results further guided the construction of several tripeptide conjugates. The binding of these compounds to RTA was studied via a luminescence-based kinetic assay, as well as through X-ray crystallography. Despite the relatively polar, solvent exposed active site, several hydrophobic interactions, most commonly π-interactions not predicted by modeling programs, were identified in all of the best-performing inhibitors. Nearly all of these compounds provide IC₅₀ values in the low micromolar range.

  DOI：

  10.1021/jm3016393

文献信息

• Peptide-Conjugated Pterins as Inhibitors of Ricin Toxin A
  作者：Ryota Saito、Jeff M. Pruet、Lawrence A. Manzano、Karl Jasheway、Arthur F. Monzingo、Paul A. Wiget、Ishan Kamat、Eric V. Anslyn、Jon D. Robertus

  DOI：10.1021/jm3016393

  日期：2013.1.10

  Several 7-peptide-substituted pterins were synthesized and tested as competitive active-site inhibitors of ricin toxin A (RTA). Focus began on dipeptide conjugates, and these results further guided the construction of several tripeptide conjugates. The binding of these compounds to RTA was studied via a luminescence-based kinetic assay, as well as through X-ray crystallography. Despite the relatively polar, solvent exposed active site, several hydrophobic interactions, most commonly π-interactions not predicted by modeling programs, were identified in all of the best-performing inhibitors. Nearly all of these compounds provide IC₅₀ values in the low micromolar range.