isopropylidene-protected diol (2R,3R)-4-N-Fmoc-amino-2,3-dihydroxybutanoic acid | 1178909-78-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: isopropylidene-protected diol (2R,3R)-4-N-Fmoc-amino-2,3-dihydroxybutanoic acid
• CAS: 1178909-78-8
• 化学式: C₂₂H₂₃NO₆
• 分子量: 397.428
• InChiKey: YINMDDDFEJMXJW-RTBURBONSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.13
• 重原子数：
  29.0
• 可旋转键数：
  5.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  94.09
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为产物：
  描述：

  D-erythronolactone acetonide 在 碳酸氢钠 、 肼 作用下， 以 1,4-二氧六环 、 乙醇 、 水 、 N,N-二甲基甲酰胺 为溶剂， 生成 isopropylidene-protected diol (2R,3R)-4-N-Fmoc-amino-2,3-dihydroxybutanoic acid
  参考文献：
  名称：

  仲氨基醇：亲和力捕获和释放中使用的无痕可裂解连接子。

  摘要：

  肽的捕获和释放通常是发现具有新颖功能的物质的途径中的关键操作。但是，有效捕获的最佳方法阻碍了释放。为了克服这一挑战，我们报道了基于仲氨基醇的接头，可在捕获后释放肽。这些氨基醇基于丝氨酸（seramox）或异丝氨酸（isoseramox），可以在固相肽合成过程中通过还原胺化将其掺入肽中。在NaIO 4下几分钟内，两个接头都被定量切割治疗。异麦角菌酯的切割产生天然肽N-末端。该连接物还显示出广泛的底物相容性。并入合成肽库后，可通过nanoLC-MS / MS鉴定所有序列。接头是细胞相容的。含有该接头的穿透细胞的肽在摄入细胞后被有效捕获并鉴定。这些发现表明，这种基于仲氨基醇的接头可能是肽发现平台的合适工具。

  DOI：

  10.1002/anie.202003478

文献信息

• Class I Major Histocompatibility Complexes Loaded by a Periodate Trigger
  作者：Boris Rodenko、Mireille Toebes、Patrick H. N. Celie、Anastassis Perrakis、Ton N. M. Schumacher、Huib Ovaa

  DOI：10.1021/ja9037565

  日期：2009.9.2

  Class I major histocompatibility complexes (MHCs) present peptide ligands on the cell surface for recognition by appropriate cytotoxic T cells. The unstable nature of unliganded MHC necessitates the production of recombinant class I complexes through in vitro refolding reactions in the presence of an added excess of peptides. This strategy is not amenable to high-throughput production of vast collections of class I complexes. To address this issue, we recently designed photocaged MHC ligands that can be cleaved by a UV light trigger in the MHC bound state under conditions that do not affect the integrity of the MHC structure. The results obtained with photocaged MHC ligands demonstrate that conditional MHC ligands can form a generally applicable concept for the creation of defined peptide-MHCs. However, the use of UV exposure to mediate ligand exchange is unsuited for a number of applications, due to the lack of UV penetration through cell culture systems and due to the transfer of heat upon UV irradiation, which can induce evaporation. To overcome these limitations, here, we provide proof-of-concept for the generation of defined peptide-MHCs by chemical trigger-induced ligand exchange. The crystal structure of the MHC with the novel chemosensitive ligand showcases that the ligand occupies the expected binding site, in a conformation where the hydroxyl groups should be reactive to periodate. We proceed to validate this technology by producing peptide-MHCs that can be used for T cell detection. The methodology that we describe here should allow loading of MHCs with defined peptides in cell culture devices, thereby permitting antigen-specific T cell expansion and purification for cell therapy. In addition, this technology will be useful to develop miniaturized assay systems for performing high-throughput screens for natural and unnatural MHC ligands.