benzyl (2S)-5-[[(3aS,4R,6R,7R,7aR)-4-[[tert-butyl(diphenyl)silyl]oxymethyl]-7-hydroxy-2,2-dimethyl-4,6,7,7a-tetrahydro-3aH-[1,3]dioxolo[4,5-c]pyran-6-yl]oxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)pentanoate | 178181-75-4

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: benzyl (2S)-5-[[(3aS,4R,6R,7R,7aR)-4-[[tert-butyl(diphenyl)silyl]oxymethyl]-7-hydroxy-2,2-dimethyl-4,6,7,7a-tetrahydro-3aH-[1,3]dioxolo[4,5-c]pyran-6-yl]oxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)pentanoate
• CAS: 178181-75-4
• 化学式: C₅₂H₅₉NO₁₀Si
• 分子量: 886.127
• InChiKey: COILOZMAILLHRT-UVKGIYGOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  7.62
• 重原子数：
  64
• 可旋转键数：
  19
• 环数：
  8.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  131
• 氢给体数：
  2
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  benzyl (2S)-5-[[(3aS,4R,6R,7R,7aR)-4-[[tert-butyl(diphenyl)silyl]oxymethyl]-7-hydroxy-2,2-dimethyl-4,6,7,7a-tetrahydro-3aH-[1,3]dioxolo[4,5-c]pyran-6-yl]oxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)pentanoate 在 palladium on activated charcoal 氢气 作用下， 以 乙酸乙酯 为溶剂， 反应 3.0h， 以93%的产率得到(2S)-5-[[(3aS,4R,6R,7R,7aR)-4-[[tert-butyl(diphenyl)silyl]oxymethyl]-7-hydroxy-2,2-dimethyl-4,6,7,7a-tetrahydro-3aH-[1,3]dioxolo[4,5-c]pyran-6-yl]oxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)pentanoic acid
  参考文献：
  名称：

  酸不稳定的保护基团用于碳水化合物部分的合成与II型胶原有关的糖肽

  摘要：

  带有甲硅烷基，异亚丙基和4-甲氧基苄基保护基的β-D-半乳糖吡喃糖基和α-D-吡喃葡萄糖基-β-D-吡喃半乳糖基已连接到氨基酸5-羟基-L-正缬氨酸上。所得的糖基化结构单元用于与II型胶原蛋白片段相关的糖肽的Fmoc固相合成，该片段在类风湿性关节炎小鼠模型中具有免疫优势。在使O-糖苷键保持完整的条件下，在固相进行酸催化的糖肽裂解过程中，用于碳水化合物部分的保护基被完全除去。

  DOI：

  10.1016/s0040-4020(98)83057-3
• 作为产物：
  描述：

  Fmoc-L-谷氨酸-α-苄酯 在 N-甲基吗啉 、 sodium tetrahydroborate 、 zinc(II) chloride 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 生成 benzyl (2S)-5-[[(3aS,4R,6R,7R,7aR)-4-[[tert-butyl(diphenyl)silyl]oxymethyl]-7-hydroxy-2,2-dimethyl-4,6,7,7a-tetrahydro-3aH-[1,3]dioxolo[4,5-c]pyran-6-yl]oxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)pentanoate
  参考文献：
  名称：

  II型胶原糖肽类似物的制备-酸不稳定的保护基用于碳水化合物部分在O型糖肽的固相合成中

  摘要：

  通过固相合成已经制备了II型胶原上的免疫显性T细胞表位的糖肽类似物。由两个带有甲硅烷基和异丙叉基保护基团的单糖单元和Fmoc 5-羟基正缬氨酸制备糖基化氨基酸对于合成至关重要。糖肽组装后，碳水化合物保护基与固相经酸催化裂解同时被去除。

  DOI：

  10.1016/0040-4039(96)00456-x

文献信息

• Preparation of a glycopeptide analogue of type II collagen — Use of acid labile protective groups for carbohydrate moieties in solid phase synthesis of O-linked glycopeptides
  作者：Johan Broddefalk、Karl-Erik Bergquist、Jan Kihlberg

  DOI：10.1016/0040-4039(96)00456-x

  日期：1996.4

  A glycopeptide analogue of the immunodominant T cell epitope on type II collagen has been prepared by solid phase synthesis. Preparation of a glycosylated amino acid from two monosaccharide units that carried silyl and isopropylidene protective groups and Fmoc 5-hydroxynorvaline was essential for the synthesis. After assembly of the glycopeptide the carbohydrate protective groups were removed simultaneously

  通过固相合成已经制备了II型胶原上的免疫显性T细胞表位的糖肽类似物。由两个带有甲硅烷基和异丙叉基保护基团的单糖单元和Fmoc 5-羟基正缬氨酸制备糖基化氨基酸对于合成至关重要。糖肽组装后，碳水化合物保护基与固相经酸催化裂解同时被去除。
• Use of acid-labile protective groups for carbohydrate moieties in synthesis of glycopeptides related to type II collagen
  作者：Johan Broddefalk、Karl-Erik Bergquist、Jan Kihlberg

  DOI：10.1016/s0040-4020(98)83057-3

  日期：1998.9

  silyl, isopropylidene and 4-methoxybenzyl protective groups have been attached to the amino acid 5-hydroxy-L-norvaline. The resulting glycosylated building blocks were used in Fmoc solid-phase synthesis of glycopeptides related to a fragment from type II collagen which is immunodominant in a mouse model for rheumatoid arthritis. The protective groups used for the carbohydrate moieties were completely removed

  带有甲硅烷基，异亚丙基和4-甲氧基苄基保护基的β-D-半乳糖吡喃糖基和α-D-吡喃葡萄糖基-β-D-吡喃半乳糖基已连接到氨基酸5-羟基-L-正缬氨酸上。所得的糖基化结构单元用于与II型胶原蛋白片段相关的糖肽的Fmoc固相合成，该片段在类风湿性关节炎小鼠模型中具有免疫优势。在使O-糖苷键保持完整的条件下，在固相进行酸催化的糖肽裂解过程中，用于碳水化合物部分的保护基被完全除去。
• T Cells Recognize a Glycopeptide Derived from Type II Collagen in a Model for Rheumatoid Arthritis
  作者：Johan Broddefalk、Johan Bäcklund、Fredrik Almqvist、Martin Johansson、Rikard Holmdahl、Jan Kihlberg

  DOI：10.1021/ja980489k

  日期：1998.8.1

  Even though most eucaryotic proteins are glycosylated, very Little is known on if, or how, the glycans influence essential immunological events such as antigen processing, major histocompatibility complex (MHC) restricted presentation, and recognition by T cells. We have used synthetic glycopeptides to elucidate the specificity of T cell hybridomas, obtained by immunization with the glycoprotein type II collagen in a mouse model for rheumatoid arthritis. To enable these studies, glycosylated and suitably protected derivatives of (5R)-5-hydroxy-L-lysine, and the similar 5-hydroxy-L-norvaline, were prepared and then used in Fmoc solid-phase synthesis of glycopeptides related to the immunodominant fragment from type II collagen, CII(256-270). Evaluation of the synthetic glycopeptides provided evidence that antigen-presenting cells can indeed process glycoproteins to glycopeptides, which elicit a T cell response when presented by class II MHC molecules. A glycopeptide carrying a single B-D-galactosyl residue attached to hydroxylysine at position 264 in the center of the CII(256-270) peptide was recognized by most of the hybridomas in a way involving specific contacts between the carbohydrate and the T cell receptor. The results suggest an explanation for the recent observation that glycosylated type II collagen induces more severe forms of arthritis in the mouse than deglycosylated type II collagen and provide additional knowledge on how rheumatoid arthritis may occur also in humans.