(2S)-N-[(2S,3R)-1-[[(2S,3R)-1-[[(2S,3R)-3-[(2S,3R,4R,5R,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-1-[(2S)-2-[[(2S,3S)-1-[[(2S)-1-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxobutan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]-1-acetylpyrrolidine-2-carboxamide | 137816-31-0

• 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: (2S)-N-[(2S,3R)-1-[[(2S,3R)-1-[[(2S,3R)-3-[(2S,3R,4R,5R,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-1-[(2S)-2-[[(2S,3S)-1-[[(2S)-1-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxobutan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]-1-acetylpyrrolidine-2-carboxamide
• CAS: 137816-31-0
• 化学式: C₄₅H₇₆N₁₀O₁₉
• 分子量: 1061.15
• InChiKey: CXNNIASDCYEUFM-PKGJIERRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.1
• 重原子数：
  74
• 可旋转键数：
  25
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.78
• 拓扑面积：
  448
• 氢给体数：
  15
• 氢受体数：
  19

反应信息

• 作为反应物：
  描述：

  (2S)-N-[(2S,3R)-1-[[(2S,3R)-1-[[(2S,3R)-3-[(2S,3R,4R,5R,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-1-[(2S)-2-[[(2S,3S)-1-[[(2S)-1-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxobutan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]-1-acetylpyrrolidine-2-carboxamide 在 sodium hydroxide 、 硼氘化钠 作用下， 反应 18.0h， 生成 AcPro-Thr-Thr-Dhb-Pro-Ile-Ser-Thr
  参考文献：
  名称：

  Determination of glycosylation sites inO-linked glycopeptides: A sensitive mass spectrometric protocol

  摘要：

  AbstractA sensitive mass spectrometric method for the specific identification of O‐glycosylation sites in glycopeptides is presented. Reductive β‐elimination liberates a peptide containing a specifically modified amino acid at the former site of carbohydrate attachment. Mass spectrometry is used to determine the sequence of the modified peptide, in which the position of the modified amino acid marks the site of O‐glycosylation. The method also provides information on the carbohydrate chain and is applicable at the low nanomolar level.

  DOI：

  10.1002/oms.1210281228