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Structural Determination of Bis-histidinopeptide Zinc Complexes by 15N NMR (HMBC) Spectra

         

摘要

@@ Polynitrogen receptors such as bis-histidine peptides possess strong ability to bind metals, which play much important roles in medicinal, bioinorganic, bioorganic, biomimetic and supramolecular chemistry. In order to investigate the interaction of these hosts with a variety of neutral, cationic and anionic guests, several techniques, for example, NMR,potentiometric tirations and monocrystal X-ray diffraction have been employed. Among them NMR is a powerful technique for unraveling the structure of polynitrogen receptors as long as they are in solution where the rapid tumbling of molecules averages out the anisotropies such as chemical shift and dipole-dipole interactions. General 1H NMR approach has been widely used for the study of host-guest interaction, but it is difficult for the accurate measurement in complexes structures, particularly metal complexes structures in which how the polynitrogen receptors bind metal, and which nitrogen binds metal and so on.

著录项

  • 来源
    《有机化学》 |2004年第z1期|380|共1页
  • 作者单位

    Department of Inorganic and Organic Chemistry, Universitat Jaume L Castellon 12080, Spain;

    School of Chemistry and Chemical Engineering, Southwest China Normal University, Chongqing 400715;

    School of Pharrnaceutical Sciences, Chongqing Medical University, Chongqing 400016;

    Department of Inorganic and Organic Chemistry, Universitat Jaume L Castellon 12080, Spain;

    Department of Inorganic and Organic Chemistry, Universitat Jaume L Castellon 12080, Spain;

    Department of Inorganic and Organic Chemistry, Universitat Jaume L Castellon 12080, Spain;

    School of Chemistry and Chemical Engineering, Southwest China Normal University, Chongqing 400715;

    School of Pharrnaceutical Sciences, Chongqing Medical University, Chongqing 400016;

  • 原文格式 PDF
  • 正文语种 chi
  • 中图分类 化学;
  • 关键词

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