cyclo(DPGNYIsSR) | 1201905-11-4

• 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: cyclo(DPGNYIsSR)
• 英文别名: cyclo[Arg-Asp-Pro-Gly-Tyr-Ile-D-Ser-Ser]；2-[(3S,6S,9S,12R,15S,18S,24S)-15-[(2S)-butan-2-yl]-6-[3-(diaminomethylideneamino)propyl]-9,12-bis(hydroxymethyl)-18-[(4-hydroxyphenyl)methyl]-2,5,8,11,14,17,20,23-octaoxo-1,4,7,10,13,16,19,22-octazabicyclo[22.3.0]heptacosan-3-yl]acetic acid
• CAS: 1201905-11-4
• 化学式: C₃₈H₅₇N₁₁O₁₃
• 分子量: 875.936
• InChiKey: XACMZIBHSWLGDY-SLHPDDFMSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.6
• 重原子数：
  62
• 可旋转键数：
  12
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  386
• 氢给体数：
  13
• 氢受体数：
  14

反应信息

• 作为产物：
  描述：

  Fmoc-Asp(OAll)-Pol 、 Fmoc-甘氨酸 、 Fmoc-L-脯氨酸 、 FMOC-O-叔丁基-L-丝氨酸 、 Fmoc-L-异亮氨酸 、 Fmoc-O-叔丁基-L-酪氨酸 、 Fmoc-O-叔丁基-D-丝氨酸 、 Fmoc-Pbf-L-精氨酸 在 哌啶 、 6-chloro-3-((dimethylamino)(dimethyliminio)methyl)-1H-benzo[d][1,2,3]triazol-3-ium-1-olatehexafluorophosphate(V) 、 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 cyclo(DPGNYIsSR)
  参考文献：
  名称：

  Conformationally Constrained Mimetics of Laminin Peptide YIGSR as Precursors for Antimetastatic Disintegrins

  摘要：

  Conformationally constrained mimetics of the laminin cell-adhesion site, YIGSR, are described. The site is the natural antagonist of the integrin-associated laminin receptor 1 (LAMR1) known to mediate metastatic tumor adhesion. The attachment of selected metastatic cell lines toward the constrained antagonists has been assessed. Observed differential responses prompted by folding preferences of the mimetics revealed stronger attachment activities for turnlike structures. The results permit the conformational design of antimetastatic disintegrins.

  DOI：

  10.1021/jm901212n

文献信息

• Conformationally Constrained Mimetics of Laminin Peptide YIGSR as Precursors for Antimetastatic Disintegrins
  作者：Angelo Bella、Helen Lewis、Jennifer Phu、Andrew R. Bottrill、Sharad C. Mistry、Christine E. Pullar、Maxim G. Ryadnov

  DOI：10.1021/jm901212n

  日期：2009.12.24

  Conformationally constrained mimetics of the laminin cell-adhesion site, YIGSR, are described. The site is the natural antagonist of the integrin-associated laminin receptor 1 (LAMR1) known to mediate metastatic tumor adhesion. The attachment of selected metastatic cell lines toward the constrained antagonists has been assessed. Observed differential responses prompted by folding preferences of the mimetics revealed stronger attachment activities for turnlike structures. The results permit the conformational design of antimetastatic disintegrins.