(2S,5R)-6-tert-Butoxycarbonylamino-5-[(3aS,4R,6R,7R,7aR)-4-(tert-butyl-diphenyl-silanyloxymethyl)-7-hydroxy-2,2-dimethyl-tetrahydro-[1,3]dioxolo[4,5-c]pyran-6-yloxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid benzyl ester | 212388-39-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: (2S,5R)-6-tert-Butoxycarbonylamino-5-[(3aS,4R,6R,7R,7aR)-4-(tert-butyl-diphenyl-silanyloxymethyl)-7-hydroxy-2,2-dimethyl-tetrahydro-[1,3]dioxolo[4,5-c]pyran-6-yloxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid benzyl ester
• CAS: 212388-39-1
• 化学式: C₅₈H₇₀N₂O₁₂Si
• 分子量: 1015.29
• InChiKey: YQNUSHFNSYFRTI-GXKSTQICSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.51
• 重原子数：
  73.0
• 可旋转键数：
  18.0
• 环数：
  8.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  169.34
• 氢给体数：
  3.0
• 氢受体数：
  12.0

反应信息

• 作为反应物：
  描述：

  (2S,5R)-6-tert-Butoxycarbonylamino-5-[(3aS,4R,6R,7R,7aR)-4-(tert-butyl-diphenyl-silanyloxymethyl)-7-hydroxy-2,2-dimethyl-tetrahydro-[1,3]dioxolo[4,5-c]pyran-6-yloxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid benzyl ester 在 palladium on activated charcoal 氢气 作用下， 以 乙酸乙酯 为溶剂， 反应 4.0h， 以85%的产率得到(2S,5R)-6-tert-Butoxycarbonylamino-5-[(3aS,4R,6R,7R,7aR)-4-(tert-butyl-diphenyl-silanyloxymethyl)-7-hydroxy-2,2-dimethyl-tetrahydro-[1,3]dioxolo[4,5-c]pyran-6-yloxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid
  参考文献：
  名称：

  T Cells Recognize a Glycopeptide Derived from Type II Collagen in a Model for Rheumatoid Arthritis

  摘要：

  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.

  DOI：

  10.1021/ja980489k
• 作为产物：
  描述：

  3,4-O-isopropylidene-6-O-tert-butyldiphenylsilyl-D-galactal 在 molecular sieve 、 二甲基二环氧乙烷 、 zinc(II) chloride 作用下， 以 二氯甲烷 、 丙酮 为溶剂， 反应 20.5h， 生成 (2S,5R)-6-tert-Butoxycarbonylamino-5-[(3aS,4R,6R,7R,7aR)-4-(tert-butyl-diphenyl-silanyloxymethyl)-7-hydroxy-2,2-dimethyl-tetrahydro-[1,3]dioxolo[4,5-c]pyran-6-yloxy]-2-(9H-fluoren-9-ylmethoxycarbonylamino)-hexanoic acid benzyl ester
  参考文献：
  名称：

  T Cells Recognize a Glycopeptide Derived from Type II Collagen in a Model for Rheumatoid Arthritis

  摘要：

  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.

  DOI：

  10.1021/ja980489k