Asn-Cys-Ser

• 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: Asn-Cys-Ser
• 英文别名: NCS；(2S)-2-[[(2R)-2-[[(2S)-2,4-diamino-4-oxobutanoyl]amino]-3-sulfanylpropanoyl]amino]-3-hydroxypropanoic acid
• 化学式: C₁₀H₁₈N₄O₆S
• 分子量: 322.342
• InChiKey: SPIPSJXLZVTXJL-ZLUOBGJFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.2
• 重原子数：
  21
• 可旋转键数：
  9
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.6
• 拓扑面积：
  186
• 氢给体数：
  7
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  Asn-Cys-Ser 在 盐酸 、 水 、 pepsin 、 Pancreatin 、 碳酸氢钠 、 sodium hydroxide 作用下， 反应 6.0h， 生成 L-丝氨酸 、 L-半胱氨酸
  参考文献：
  名称：

  Degradation and antioxidant activities of peptides and zinc–peptide complexes during in vitro gastrointestinal digestion

  摘要：

  The degradation characteristics of three peptides (Ser-Met, Asn-Cys-Ser, and glutathione) and their zinc-peptide complexes were studied using a two-stage in vitro digestion model. Enzyme-resistant peptides and zinc-peptide complexes, antioxidant activities, and free amino acids released by digestive enzymes, were measured in this study. The results revealed that the three peptides and their zinc-peptide complexes were resistant to pepsin but not to pancreatin. Pancreatin can partly hydrolyse both peptides and zinc-peptide complexes, but more than half of them remaining in their original form after gastrointestinal digestion. The coordination of zinc improved the enzymatic resistance of the peptide due to lower solubility of complexes and affected the hydrolytic site of pepsin and pancreatin. Zinc-Asn-Cys-Ser, which is highly resistant to enzymatic hydrolysis and maintains Zn in a soluble form, may have potential to improve Zn bioavailability. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.foodchem.2014.10.066

文献信息

• Degradation and antioxidant activities of peptides and zinc–peptide complexes during in vitro gastrointestinal digestion
  作者：Chan Wang、Bo Li、Bo Wang、Ningning Xie

  DOI：10.1016/j.foodchem.2014.10.066

  日期：2015.4

  The degradation characteristics of three peptides (Ser-Met, Asn-Cys-Ser, and glutathione) and their zinc-peptide complexes were studied using a two-stage in vitro digestion model. Enzyme-resistant peptides and zinc-peptide complexes, antioxidant activities, and free amino acids released by digestive enzymes, were measured in this study. The results revealed that the three peptides and their zinc-peptide complexes were resistant to pepsin but not to pancreatin. Pancreatin can partly hydrolyse both peptides and zinc-peptide complexes, but more than half of them remaining in their original form after gastrointestinal digestion. The coordination of zinc improved the enzymatic resistance of the peptide due to lower solubility of complexes and affected the hydrolytic site of pepsin and pancreatin. Zinc-Asn-Cys-Ser, which is highly resistant to enzymatic hydrolysis and maintains Zn in a soluble form, may have potential to improve Zn bioavailability. (C) 2014 Elsevier Ltd. All rights reserved.