泡蛙肽 | 2507-24-6

• 物质功能分类: 生物化工 - 多肽
• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 中文名称: 泡蛙肽
• 英文名称: physalaemin
• 英文别名: Physalemin；(3S)-4-[(2S)-2-[[(2S)-4-amino-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S)-1-amino-4-methylsulfanyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-1-oxohexan-2-yl]amino]-1,4-dioxobutan-2-yl]carbamoyl]pyrrolidin-1-yl]-4-oxo-3-[[(2S)-2-[[(2S)-5-oxopyrrolidine-2-carbonyl]amino]propanoyl]amino]butanoic acid
• CAS: 2507-24-6
• 化学式: C₅₈H₈₄N₁₄O₁₆S
• 分子量: 1265.46
• InChiKey: SHSUJLMLURFKID-YFUSJSQUSA-N

物化性质

• 溶解度：
  溶于二甲基亚砜

计算性质

• 辛醇/水分配系数(LogP)：
  -4.2
• 重原子数：
  89
• 可旋转键数：
  37
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.55
• 拓扑面积：
  506
• 氢给体数：
  15
• 氢受体数：
  18

安全信息

• WGK Germany：
  3

制备方法与用途

用途

Physalaemin最初是从Physalaemus frog中分离出来的，是一种与P物质密切相关的速激肽。它是一种有效的血管扩张剂，具有降压作用。

生物活性

Physalaemin是一种非哺乳动物类的速激肽，选择性地高亲和力结合到神经激肽-1 (NK1) 受体。

靶点

神经激肽-1 (NK1) 受体

体外研究

Physalaemin（PHY）是一种十一肽，具有序列pGlu-Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly-Leu-Met-NH2，是tachykinin家族神经肽的一员。PHY在功能和化学组成上与哺乳动物的速激肽物质P（SP）非常接近，而SP已经广泛研究并被充分表征。Physalaemin是一种缓激肽增强肽（BPP-5a）。

反应信息

• 作为反应物：
  描述：

  泡蛙肽 在 glass 作用下， 以 水 为溶剂， 生成 (S)-2-{(S)-2-[((S)-5-Oxo-pyrrolidine-2-carbonyl)-amino]-propionylamino}-succinic acid 、 Pro-Asn-Lys-Phe-Tyr-Gly-Leu-Met-NH2
  参考文献：
  名称：

  摘要：

  Purpose. To investigate chemical reactivity in water soluble glasses.Methods. Rates of bond cleavage reactions in freeze-dried and freeze-concentrated aqueous carbohydrate solutions were measured above and below the glass transition temperatures (T(g)). The kinetics of two reactions have been determined in formulations containing di-and polysaccharides: (1) fission of the Asp-Pro peptide bond in Physalaemin and Hamburger peptide by following the release of proline, using a ninhydrin based reaction and (2) the unimolecular dissociation of 2(4-nitrophenoxy) tetrahydropyran by following the release of the 4-nitrophenoxy anion.Results, The results show dearly that reaction occurs below the glass transition temperature, albeit at very reduced rates. No significant enhancement of the temperature dependence of the rate constant was observed near T,. Different water soluble glasses provide different degrees of stability. The order of stabilisation was sucrose>Ficoll (low mel. weight)>Byco A congruent to Ficoll (high mel. weight)>dextran. The density of the matrix, and therefore the degrees of freedom of mobility of the reactant, is thought to be responsible for these differences.Conclusions. The storage of therapeutic agents, such as proteins, in glassy matrices below T, does not confer indefinite stability. When formulating products, notice should be taken of the differing stabilisation properties of excipients.

  DOI：

  10.1023/a:1011912228954

文献信息

• ——
  作者：Lisette Streefland、Anthony D. Auffret、Felix Franks

  DOI：10.1023/a:1011912228954

  日期：——

  Purpose. To investigate chemical reactivity in water soluble glasses.Methods. Rates of bond cleavage reactions in freeze-dried and freeze-concentrated aqueous carbohydrate solutions were measured above and below the glass transition temperatures (T(g)). The kinetics of two reactions have been determined in formulations containing di-and polysaccharides: (1) fission of the Asp-Pro peptide bond in Physalaemin and Hamburger peptide by following the release of proline, using a ninhydrin based reaction and (2) the unimolecular dissociation of 2(4-nitrophenoxy) tetrahydropyran by following the release of the 4-nitrophenoxy anion.Results, The results show dearly that reaction occurs below the glass transition temperature, albeit at very reduced rates. No significant enhancement of the temperature dependence of the rate constant was observed near T,. Different water soluble glasses provide different degrees of stability. The order of stabilisation was sucrose>Ficoll (low mel. weight)>Byco A congruent to Ficoll (high mel. weight)>dextran. The density of the matrix, and therefore the degrees of freedom of mobility of the reactant, is thought to be responsible for these differences.Conclusions. The storage of therapeutic agents, such as proteins, in glassy matrices below T, does not confer indefinite stability. When formulating products, notice should be taken of the differing stabilisation properties of excipients.