(2S)-2-amino-6-((6R,7S)-2-(((S)-4-amino-4-carboxybutyl)amino)-6,7-dihydroxy-6,7,8,8a-tetrahydroimidazo[4,5-b]azepin-4(5H)-yl)hexanoic acid | 257290-23-6

• 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)-2-amino-6-((6R,7S)-2-(((S)-4-amino-4-carboxybutyl)amino)-6,7-dihydroxy-6,7,8,8a-tetrahydroimidazo[4,5-b]azepin-4(5H)-yl)hexanoic acid
• 英文别名: 2-ammonio-6-{2-[(4-ammonio-5-oxido-5-oxopentyl)amino]-6,7-dihydroxy-4,5,6,7,8,8a-hexahydroimidazo[4,5-b]azepin-4-yl}hexanoate；glucosepane；Glucosepane；(2S)-2-amino-6-[(6R,7S)-2-[(4S)-4-amino-4-carboxybutyl]imino-6,7-dihydroxy-1,5,6,7,8,8a-hexahydroimidazo[4,5-b]azepin-4-yl]hexanoic acid
• CAS: 257290-23-6
• 化学式: C₁₈H₃₂N₆O₆
• 分子量: 428.489
• InChiKey: JTMICRULXGWYCN-WSOGJNRSSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -7.1
• 重原子数：
  30
• 可旋转键数：
  11
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.78
• 拓扑面积：
  207
• 氢给体数：
  7
• 氢受体数：
  9

反应信息

• 作为产物：
  描述：

  N-alpha-叔丁氧羰基-L-赖氨酸 在 盐酸 作用下， 以 水 为溶剂， 反应 17.5h， 生成 (2S)-2-amino-6-((6R,7S)-2-(((S)-4-amino-4-carboxybutyl)amino)-6,7-dihydroxy-6,7,8,8a-tetrahydroimidazo[4,5-b]azepin-4(5H)-yl)hexanoic acid
  参考文献：
  名称：

  Cross-linking of proteins by maillard processes—characterization and detection of a lysine-arginine cross-link derived from d-glucose

  摘要：

  Covalently cross-linked proteins are among the major modifications caused by the advanced Maillard reaction. So far, the chemical nature of these aggregates is largely unknown. Investigations are reported on how the cross-linking unit 2-ammonio-6-{2-[(4-ammonio-5-oxido-5-oxopentyl)amino]-6,7-dihydroxy-4,5,6,7,8,8a-hexahydroimidazo [4,5-b]azepin-4-yl} hexanoate (7), designated as glucosepan, can be identified and quantified from D-glucose-bovine serum albumin (BSA) incubations. Independent synthesis and unequivocal structural characterization are given for glucosepan 7. A protocol was established for its determination by LC-MS with electrospray ionization (ESI). BSA and D-glucose were incubated at 37 degrees C, pH 7.4 for eight weeks and the time-dependent formation of 7 was observed. Since glucosepan 7 is unstable under acid proteolytic conditions, BSA was cleaved enzymatically. The maximum value obtained from a solution containing 50 g/L BSA and 100 mM D-glucose after eight weeks incubation time corresponds to an arginine derivatization rate of 1.38 +/- 0.07 mmol 7/mol Arg (equivalent to 31.7 +/- 1.6 mmol 7/mol BSA). From these results, it seems justified to expect 7 to play an important role in the cross-linking of proteins in vivo as well as in foodstuffs. The structural similarity of glucosepan 7 and pentosidine 1 made it obvious to also look for an eventual parallelism in the respective formation pathways. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(99)00040-1

文献信息

• [EN] ADVANCED GLYCATION END-PRODUCT BREAKING BIOCATALYSTS<br/>[FR] BIOCATALYSEURS DE RUPTURE DE PRODUITS FINAUX DE GLYCATION AVANCÉE
  申请人：UNIV YALE

  公开号：WO2020215043A1

  公开（公告）日：2020-10-22

  In various aspects and embodiments the invention provides compositions and methods for removing glucosepane from one or more proteins in a subject. In certain embodiments, the method comprises administering to the subject an effective amount of a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOs: 1-13, or a biologically active fragment thereof.

  在各个方面和实施方式中，该发明提供了用于从受体中的一个或多个蛋白质中去除葡萄糖胺的组合物和方法。在某些实施方式中，该方法包括向受体施用包含从以下序列中选择的氨基酸序列的多肽的有效量，该序列包括SEQ ID NOs: 1-13，或其生物活性片段。
• Cross-linking of proteins by maillard processes—characterization and detection of a lysine-arginine cross-link derived from d-glucose
  作者：Markus O Lederer、Holger P Bühler

  DOI：10.1016/s0968-0896(99)00040-1

  日期：1999.6

  Covalently cross-linked proteins are among the major modifications caused by the advanced Maillard reaction. So far, the chemical nature of these aggregates is largely unknown. Investigations are reported on how the cross-linking unit 2-ammonio-6-2-[(4-ammonio-5-oxido-5-oxopentyl)amino]-6,7-dihydroxy-4,5,6,7,8,8a-hexahydroimidazo [4,5-b]azepin-4-yl} hexanoate (7), designated as glucosepan, can be identified and quantified from D-glucose-bovine serum albumin (BSA) incubations. Independent synthesis and unequivocal structural characterization are given for glucosepan 7. A protocol was established for its determination by LC-MS with electrospray ionization (ESI). BSA and D-glucose were incubated at 37 degrees C, pH 7.4 for eight weeks and the time-dependent formation of 7 was observed. Since glucosepan 7 is unstable under acid proteolytic conditions, BSA was cleaved enzymatically. The maximum value obtained from a solution containing 50 g/L BSA and 100 mM D-glucose after eight weeks incubation time corresponds to an arginine derivatization rate of 1.38 +/- 0.07 mmol 7/mol Arg (equivalent to 31.7 +/- 1.6 mmol 7/mol BSA). From these results, it seems justified to expect 7 to play an important role in the cross-linking of proteins in vivo as well as in foodstuffs. The structural similarity of glucosepan 7 and pentosidine 1 made it obvious to also look for an eventual parallelism in the respective formation pathways. (C) 1999 Elsevier Science Ltd. All rights reserved.