L-tryptophan-taurine | 1460283-82-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吲哚及其衍生物
• 英文名称: L-tryptophan-taurine
• 英文别名: Ethanesulfonic acid, 2-[[(2S)-2-amino-3-(1H-indol-3-yl)-1-oxopropyl]amino]-；2-[[(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]amino]ethanesulfonic acid
• CAS: 1460283-82-2
• 化学式: C₁₃H₁₇N₃O₄S
• 分子量: 311.362
• InChiKey: PQVKUUFDUQXKSS-NSHDSACASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.04
• 重原子数：
  21.0
• 可旋转键数：
  6.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  125.28
• 氢给体数：
  4.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  L-tryptophan-taurine 、 己二酸 1,6-二(2,5-二氧代-1-吡咯烷基)酯 在 碳酸氢钠 作用下， 以 1,4-二氧六环 、 水 为溶剂， 反应 24.0h， 以67%的产率得到
  参考文献：
  名称：

  Inhibition of Human and Bovine Insulin Fibril Formation by Designed Peptide Conjugates

  摘要：

  The aggregation of insulin, to afford amyloidogenic fibers, is a well-studied phenomenon, which has interesting biological ramifications and pharmaceutical implications. These fibers have been ascribed an intriguing role in certain disease states and stability of pharmaceutical formulations of this hormone. The present study describes the design and inhibitory effects of novel peptide conjugates toward fibrillation of insulin as investigated by thioflavin T assay, circular dichroism (CD), and atomic force microscopy (AFM). Possible interaction of insulin with peptide-based fibrillation inhibitors is also probed by other solution phase studies, which reveal an important role of aromatic pi-pi interactions in the inhibition process. CD studies suggest that a freshly prepared solution of insulin, rich in a-helices, transforms into a beta-sheet structure upon aggregation, which gets perturbed in the presence of synthesized inhibitors. Therefore, these newly designed peptides could serve as potential leads as inhibitors of insulin aggregation.

  DOI：

  10.1021/mp400364w
• 作为产物：
  描述：

  N-叔丁氧羰基-L-色氨酸 在 碳酸氢钠 、 N,N'-二环己基碳二亚胺 作用下， 以 1,4-二氧六环 、 二氯甲烷 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 24.0h， 生成 L-tryptophan-taurine
  参考文献：
  名称：

  Inhibition of Human and Bovine Insulin Fibril Formation by Designed Peptide Conjugates

  摘要：

  The aggregation of insulin, to afford amyloidogenic fibers, is a well-studied phenomenon, which has interesting biological ramifications and pharmaceutical implications. These fibers have been ascribed an intriguing role in certain disease states and stability of pharmaceutical formulations of this hormone. The present study describes the design and inhibitory effects of novel peptide conjugates toward fibrillation of insulin as investigated by thioflavin T assay, circular dichroism (CD), and atomic force microscopy (AFM). Possible interaction of insulin with peptide-based fibrillation inhibitors is also probed by other solution phase studies, which reveal an important role of aromatic pi-pi interactions in the inhibition process. CD studies suggest that a freshly prepared solution of insulin, rich in a-helices, transforms into a beta-sheet structure upon aggregation, which gets perturbed in the presence of synthesized inhibitors. Therefore, these newly designed peptides could serve as potential leads as inhibitors of insulin aggregation.

  DOI：

  10.1021/mp400364w