(1,4,7,10,13,16-hexaoxacyclooctadecan-2-yl)methyl 4-iodobenzoate | 1287753-20-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (1,4,7,10,13,16-hexaoxacyclooctadecan-2-yl)methyl 4-iodobenzoate
• CAS: 1287753-20-1
• 化学式: C₂₀H₂₉IO₈
• 分子量: 524.35
• InChiKey: ASCFWNHNNVUFDD-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.93
• 重原子数：
  29.0
• 可旋转键数：
  3.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.65
• 拓扑面积：
  81.68
• 氢给体数：
  0.0
• 氢受体数：
  8.0

反应信息

• 作为产物：
  描述：

  4-碘苯甲酸 、 2-羟甲基-18-冠-6 在 4-二甲氨基吡啶 、 N,N'-二环己基碳二亚胺 作用下， 以 1,4-二氧六环 为溶剂， 反应 12.0h， 生成 (1,4,7,10,13,16-hexaoxacyclooctadecan-2-yl)methyl 4-iodobenzoate
  参考文献：
  名称：

  Rapid, quantitative, and site specific synthesis of biomolecular radicals from a simple photocaged precursor

  摘要：

  研究表明，新型对碘苯甲酸酯类标记试剂是一种有效的光致前体，可在气态和凝聚态中选择性地合成生物分子自由基。在真空中，单脉冲紫外光子（266 纳米）就足以定量光解 C-I 键。在水溶液中，用 15 瓦紧凑型荧光灯（254 纳米）照射，光解半衰期估计为 2.5 分钟。

  DOI：

  10.1039/c0cc03363d

文献信息

• Dynamic Interchanging Native States of Lymphotactin Examined by SNAPP-MS
  作者：Qingyu Sun、Robert C. Tyler、Brian F. Volkman、Ryan R. Julian

  DOI：10.1007/s13361-010-0042-3

  日期：2011.3.1

  The human chemokine lymphotactin (Ltn) is a remarkable protein that interconverts between two unrelated native state structures in the condensed phase. It is possible to shift the equilibrium toward either conformation with selected sequence substitutions. Previous results have shown that a disulfide-stabilized variant preferentially adopts the canonical chemokine fold (Ltn10), while a single amino acid change (W55D) favors the novel Ltn40 dimeric structure. Selective noncovalent adduct protein probing (SNAPP) is a recently developed method for examining solution phase protein structure. Herein, it is demonstrated that SNAPP can easily recognize and distinguish between the Ltn10 and Ltn40 states of lymphotactin in aqueous solution. The effects of organic denaturants, acid, and disulfide bond reduction and blocking were also examined using SNAPP for the CC3, W55D, and wild type proteins. Only disulfide reduction was shown to significantly perturb the protein, and resulted in considerably decreased adduct formation consistent with loss of tertiary/secondary structure. Cold denaturation experiments demonstrated that wild-type Ltn is the most temperature sensitive of the three proteins. Examination of the higher charge states in all experiments, which are presumed to represent transition state structures between Ltn-10 and Ltn-40, reveals increased 18C6 attachment relative to the more folded structures. This observation is consistent with increased competitive intramolecular hydrogen bonding, which may guide the transition. Experiments examining the gas phase structures revealed that all three proteins can be structurally distinguished in the gas phase. In addition, the gas phase experiments enabled identification of preferred adduct binding sites.

  人类趋化因子淋巴素（Ltn）是一种卓越的蛋白质，在凝聚相中可在两种不相关的天然状态结构之间相互转换。通过选择序列替换，可以改变平衡，使其向任一构象转变。先前的研究结果表明，二硫键稳定变体倾向于采用典型的趋化因子折叠（Ltn10），而单个氨基酸变化（W55D）则有利于新的Ltn40二聚体结构。选择性非共价加合物蛋白质探测（SNAPP）是最近开发的一种用于研究溶液相蛋白质结构的方法。本文证明了SNAPP可以轻松识别并区分水溶液中淋巴素的Ltn10和Ltn40状态。此外，还使用SNAPP对CC3、W55D和野生型蛋白质进行了有机变性剂、酸和二硫键还原和阻断的影响研究。结果表明，只有二硫键还原会显著干扰蛋白质，并导致加合物形成大大减少，这与三级/二级结构的丧失一致。冷变性实验表明，在三种蛋白质中，野生型Ltn对温度最敏感。在所有实验中，假设较高电荷状态代表Ltn-10和Ltn-40之间的过渡状态结构，结果表明，与折叠结构相比，18C6的附着增加。这一观察结果与分子内氢键竞争增加一致，这可能指导过渡。研究气相结构的实验表明，在气相中，三种蛋白质在结构上可以区分。此外