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N-(2-(2-Hydroxyethoxy)ethyl)-(2-naphthoxy)acetamide

中文名称
——
中文别名
——
英文名称
N-(2-(2-Hydroxyethoxy)ethyl)-(2-naphthoxy)acetamide
英文别名
N-[2-(2-hydroxyethoxy)ethyl]-2-naphthalen-2-yloxyacetamide
N-(2-(2-Hydroxyethoxy)ethyl)-(2-naphthoxy)acetamide化学式
CAS
——
化学式
C16H19NO4
mdl
——
分子量
289.331
InChiKey
AJLGLGIMMXBYBK-UHFFFAOYSA-N
BEILSTEIN
——
EINECS
——
  • 物化性质
  • 计算性质
  • ADMET
  • 安全信息
  • SDS
  • 制备方法与用途
  • 上下游信息
  • 反应信息
  • 文献信息
  • 表征谱图
  • 同类化合物
  • 相关功能分类
  • 相关结构分类

计算性质

  • 辛醇/水分配系数(LogP):
    1.4
  • 重原子数:
    21
  • 可旋转键数:
    8
  • 环数:
    2.0
  • sp3杂化的碳原子比例:
    0.31
  • 拓扑面积:
    67.8
  • 氢给体数:
    2
  • 氢受体数:
    4

反应信息

  • 作为产物:
    描述:
    (2-萘氧基)醋酸N-羟基丁二酰亚胺酯二甘醇胺二氯甲烷 为溶剂, 反应 3.0h, 以75%的产率得到N-(2-(2-Hydroxyethoxy)ethyl)-(2-naphthoxy)acetamide
    参考文献:
    名称:
    Using affinity capillary electrophoresis to identify the peptide in a peptide library that binds most tightly to vancomycin
    摘要:
    This paper describes a procedure, based on competitive binding, for identifying tight-binding ligand(s) for a receptor in mixtures of equimolar ligand candidates using affinity capillary electrophoresis (ACE). Vancomycin and a small library of 32 peptides were used as a model system to illustrate the procedure. This procedure should be applicable to peptide mixtures of greater complexity than the one used here, as well as to mixtures of nonpeptidic compounds. Limits and limitations to the procedure are described.
    DOI:
    10.1021/jo00055a017
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文献信息

  • Using affinity capillary electrophoresis to identify the peptide in a peptide library that binds most tightly to vancomycin
    作者:Yen Ho Chu、Luis Z. Avila、Hans A. Biebuyck、George M. Whitesides
    DOI:10.1021/jo00055a017
    日期:1993.1
    This paper describes a procedure, based on competitive binding, for identifying tight-binding ligand(s) for a receptor in mixtures of equimolar ligand candidates using affinity capillary electrophoresis (ACE). Vancomycin and a small library of 32 peptides were used as a model system to illustrate the procedure. This procedure should be applicable to peptide mixtures of greater complexity than the one used here, as well as to mixtures of nonpeptidic compounds. Limits and limitations to the procedure are described.
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