ε-N-lactulosyllysine

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 糖脂
• 英文名称: ε-N-lactulosyllysine
• 英文别名: (2S)-2-amino-6-[[(3S,4R,5R)-3,5,6-trihydroxy-2-oxo-4-[(2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyhexyl]amino]hexanoic acid
• 化学式: C₁₈H₃₄N₂O₁₂
• 分子量: 470.474
• InChiKey: XVJNMIGVIYENHK-VZJOFNIXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -7.1
• 重原子数：
  32
• 可旋转键数：
  15
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.89
• 拓扑面积：
  253
• 氢给体数：
  10
• 氢受体数：
  14

反应信息

• 作为产物：
  描述：

  N-EPSILON-乙酰-L-赖胺基乙酸 、 β-乳糖 以 甲醇 、 二甲基亚砜 为溶剂， 反应 8.0h， 生成 ε-N-lactulosyllysine
  参考文献：
  名称：

  Studies on N-Terminal Glycation of Peptides in Hypoallergenic Infant Formulas:  Quantification of α-N-(2-Furoylmethyl) Amino Acids

  摘要：

  To obtain information about the extent of the early Maillard reaction between the N-termini of peptides and lactose, alpha-N-(2-furoylmethyl) amino acids (FMAAs) were quantified together with is an element of-N-(2-furoylmethyl) lysine (furosine) in acid hydrolyzates of hypoallergenic infant formulas, conventional infant formulas, and human milk samples using RP-HPLC with UV-detection. FMAAs are formed during acid hydrolysis of peptide-bound N-terminal Amadori products (APs), and furosine is formed from the Amadori products of peptide-bound lysine. Unambiguous identification was achieved by means of LC/MS and UV-spectroscopy using independently prepared reference material. The extent of acid-induced conversion of APs to FMAAs was studied by RP-HPLC with chemiluminescent nitrogen detection (CLND). Depending on the corresponding alpha-N-lactulosyl amino acid, between 6.0% and 18.1% of FMAAs were formed during hydrolysis for 23 h at 110 degrees C in 8 N HCl. From is an element of-N-lactulosyllysine, 50% furosine is formed under these conditions. Whereas furosine was detectable in all assayed samples, five different FMAAs, alpha-FM-Lys, alpha-FM-Ala, alpha-FM-Val, alpha-FM-Ile, and alpha-FM-Leu, were exclusively detected in acid hydrolyzates of hypoallergenic infant formulas in amounts ranging from 35 to 396 mu mol/100 g protein. Taking the conversion factors into account, modification of N-terminal amino acids in peptides by reducing carbohydrates was between 0.3% and 8.4%. This has to be considered within the discussion concerning the nutritional quality of peptide- containing foods.

  DOI：

  10.1021/jf061821b

文献信息

• Studies on N-Terminal Glycation of Peptides in Hypoallergenic Infant Formulas:  Quantification of α-<i>N</i>-(2-Furoylmethyl) Amino Acids
  作者：Ilka Penndorf、Daniela Biedermann、Sarah V. Maurer、Thomas Henle

  DOI：10.1021/jf061821b

  日期：2007.2.1

  To obtain information about the extent of the early Maillard reaction between the N-termini of peptides and lactose, alpha-N-(2-furoylmethyl) amino acids (FMAAs) were quantified together with is an element of-N-(2-furoylmethyl) lysine (furosine) in acid hydrolyzates of hypoallergenic infant formulas, conventional infant formulas, and human milk samples using RP-HPLC with UV-detection. FMAAs are formed during acid hydrolysis of peptide-bound N-terminal Amadori products (APs), and furosine is formed from the Amadori products of peptide-bound lysine. Unambiguous identification was achieved by means of LC/MS and UV-spectroscopy using independently prepared reference material. The extent of acid-induced conversion of APs to FMAAs was studied by RP-HPLC with chemiluminescent nitrogen detection (CLND). Depending on the corresponding alpha-N-lactulosyl amino acid, between 6.0% and 18.1% of FMAAs were formed during hydrolysis for 23 h at 110 degrees C in 8 N HCl. From is an element of-N-lactulosyllysine, 50% furosine is formed under these conditions. Whereas furosine was detectable in all assayed samples, five different FMAAs, alpha-FM-Lys, alpha-FM-Ala, alpha-FM-Val, alpha-FM-Ile, and alpha-FM-Leu, were exclusively detected in acid hydrolyzates of hypoallergenic infant formulas in amounts ranging from 35 to 396 mu mol/100 g protein. Taking the conversion factors into account, modification of N-terminal amino acids in peptides by reducing carbohydrates was between 0.3% and 8.4%. This has to be considered within the discussion concerning the nutritional quality of peptide- containing foods.