甘氨酰甘氨酰酪氨酰-精氨酸 | 70195-20-9

• 物质功能分类: 生物化工 - 氨基酸及其衍生物
• 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
• 中文名称: 甘氨酰甘氨酰酪氨酰-精氨酸
• 英文名称: Gly-Gly-Tyr-Arg
• 英文别名: GGYR；(2S)-2-[[(2S)-2-[[2-[(2-aminoacetyl)amino]acetyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid
• CAS: 70195-20-9
• 化学式: C₁₉H₂₉N₇O₆
• 分子量: 451.483
• InChiKey: FJPHHBGPPJXISY-KBPBESRZSA-N

物化性质

• 溶解度：
  不溶于乙醇； DMSO 中≥45.1 mg/mL；水中≥90.4 mg/mL

计算性质

• 辛醇/水分配系数(LogP)：
  -4.5
• 重原子数：
  32
• 可旋转键数：
  13
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  235
• 氢给体数：
  8
• 氢受体数：
  8

安全信息

• 危险性防范说明：
  P261,P305+P351+P338
• 危险性描述：
  H302,H315,H319,H335

反应信息

• 作为反应物：
  描述：

  、 甘氨酰甘氨酰酪氨酰-精氨酸 以 水 、 N,N-二甲基甲酰胺 为溶剂， 生成
  参考文献：
  名称：

  基于C60的活性酯的制备以及C60部分与胺或醇的偶联。

  摘要：

  我们报告了基于C（60）的活性酯的合成及其C（60）部分与各种胺或醇的偶联。通过用N-羟基琥珀酰亚胺（NHS）或五氟苯酚（PFP）进行酯化反应活化甲基[60]富勒烯羧酸，并分离出活性酯。活性酯与胺或醇的反应容易进行，得到各种具有C（60）部分的化合物。

  DOI：

  10.1016/j.bmcl.2007.11.065

文献信息

• Improvement of Intestinal Absorption of Peptide Drugs by Glycosylation: Transport of Tetrapeptide by the Sodium Ion-Dependent D-Glucose Transporter
  作者：Masahiro Nomoto、Kazuhito Yamada、Makoto Haga、Masahiro Hayashi

  DOI：10.1021/js970269p

  日期：1998.3

  A tetrapeptide (Gly-Gly-Tyr-Arg, GGYR), which is not transported by di- or tripeptide transporters, was glycosylated with p-(succinylamido)phenyl alpha- or beta-D-glucopyranoside (alpha,beta-SAPG) to investigate whether these glycosylated molecules are transported by the Na+-dependent D-glucose transporter. Their uptake into brush-border membrane vesicles (BBMVs) and transport through the intestinal membrane were examined using the rapid filtration technique and the everted sac method. It was observed that glycosylation at the alpha-amino position of GGYR increased resistance to aminopeptidase activity and inhibited its degradation. When alpha- and beta-SAPG-GGYR were incubated with BBMVs, overshoot uptake was observed about 2 min after the start of incubation in the presence of an inward Na+ gradient. This uptake remained unaffected by the addition of GGYR while it was significantly inhibited when Na+ was replaced with K+ or alpha- and beta-SAPG-GGYR were incubated with BBMVs at 4 degrees C. Uptake was also markedly inhibited either with 1 mM phloridzin or 10 mM D-glucose. These findings suggested that the Na+-dependent glucose transporter (SGLT-1) played an important role in the uptake of both alpha- and beta-SAPG-GGYR into BBMVs. A comparison of alpha- with beta-SAPG-GGYR revealed that the amount of beta-SAPG-GGYR taken up was greater than that of alpha-SAPG-GGYR. From the everted sac method data, it was shown that the elimination clearance from the mucosal side, CLel, and permeation clearance to the serosal side, CLp, were 15.82 +/- 6.83 and 0.83 +/- 0.06 mu l/min/cm for alpha-SAPG-GGYR and 44.52 +/- 3.61 and 3.50 +/- 0.81 mu L/min/cm for beta-SAPG-GGYR, respectively, and that alpha-SAPG-GGYR was more resistant to enzymatic degradation than beta-SAPG-GGYR. Permeation of both alpha- and beta-SAPG-GGYR was inhibited in the presence of D-glucose and in the absence of a Na+ gradient, suggesting that both alpha- and beta-SAPG-GGYR were transported by the Na+-dependent D-glucose transporter. The permeation clearance transported by the Na+-dependent D-glucose transporter, (CLp)(Na+) of beta-SAPG-GGYR was about 5 times greater than that for alpha-SAPG-GGYR. This result may be ascribable to the fact that the beta-form of glucose has higher affinity to SGLT-1 than the alpha-form. The results of the present study encourage further investigations on improvements in intestinal absorption of peptide drugs by glycosylation.