N-(3-Sulfanylpropanoyl)-1,7-diaminoheptane | 266359-78-8

• 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: N-(3-Sulfanylpropanoyl)-1,7-diaminoheptane
• CAS: 266359-78-8
• 化学式: C₁₀H₂₂N₂OS
• 分子量: 218.363
• InChiKey: HZPGGWARQJQNRT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.33
• 重原子数：
  14.0
• 可旋转键数：
  9.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.9
• 拓扑面积：
  55.12
• 氢给体数：
  3.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  (+)生物素-N-琥珀酰亚胺基酯 、 N-(3-Sulfanylpropanoyl)-1,7-diaminoheptane 在 三乙胺 作用下， 以 氯仿 为溶剂， 反应 168.0h， 以10%的产率得到5-(6,8-Diaza-7-oxo-3-thiabicyclo[3.3.0]oct-2-yl)-N[7-(3-{[2-(N-{7-[5-(6,8-diaza-7-oxo-3-thiabicyclo[3.3.0]oct-2-yl)pentanoylamino]heptyl}carbamoyl)ethyl]disulfanyl}propanoylamino)heptyl]pentanamide
  参考文献：
  名称：

  Characterization of Protein Aggregated Gold Nanocrystals

  摘要：

  This paper describes the preparation of an aqueous dispersion of electrostatically stabilized gold nanocrystals. It also describes the characterization of these nanocrystals by NMR, SAXS, SLS, and TEM prior to and following their modification by chemisorption of 3-mecaptopropanoic acid. Using the insights gained, these nanocrystals were subsequently modified by chemisorption and appropriate surface concentration of a disulfide biotin analogue (DSBA). Addition of streptavidin to the DSBA-modified gold dispersion results in the binding of gold nanocrystals to opposite faces of the protein and in the aggregation of the dispersion. The growth kinetics and structure of the resulting aggregates were characterized by W-visible spectroscopy, DLS, SAXS, and TEM. Some implications of these findings for the assembly of complex nanocrystal architectures in solution are considered.

  DOI：

  10.1021/jp992842u
• 作为产物：
  描述：

  1-叔丁氧羰基-1,7-二氨基庚烷 在 盐酸 、 三乙胺 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 24.5h， 生成 N-(3-Sulfanylpropanoyl)-1,7-diaminoheptane
  参考文献：
  名称：

  Characterization of Protein Aggregated Gold Nanocrystals

  摘要：

  This paper describes the preparation of an aqueous dispersion of electrostatically stabilized gold nanocrystals. It also describes the characterization of these nanocrystals by NMR, SAXS, SLS, and TEM prior to and following their modification by chemisorption of 3-mecaptopropanoic acid. Using the insights gained, these nanocrystals were subsequently modified by chemisorption and appropriate surface concentration of a disulfide biotin analogue (DSBA). Addition of streptavidin to the DSBA-modified gold dispersion results in the binding of gold nanocrystals to opposite faces of the protein and in the aggregation of the dispersion. The growth kinetics and structure of the resulting aggregates were characterized by W-visible spectroscopy, DLS, SAXS, and TEM. Some implications of these findings for the assembly of complex nanocrystal architectures in solution are considered.

  DOI：

  10.1021/jp992842u