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Structural Determination of Bis-histidinopeptide Zinc Complexes by 15N NMR (HMBC) Spectra
作者姓名:ZHOU  Cheng-He  Juan F.Miravet  M.Isabel Burguete  Santiago V.Luis  BAI  Xue  YUAN  Yong
作者单位:ZHOU,Cheng-He(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)  Juan F.Miravet(Department of Inorganic and Organic Chemistry, Universitat Jaume L Castellon 12080, Spain)  M.Isabel Burguete(Department of Inorganic and Organic Chemistry, Universitat Jaume L Castellon 12080, Spain)  Santiago V.Luis(Department of Inorganic and Organic Chemistry, Universitat Jaume L Castellon 12080, Spain)  BAI,Xue(School of Chemistry and Chemical Engineering, Southwest China Normal University, Chongqing 400715)  YUAN,Yong(School of Pharrnaceutical Sciences, Chongqing Medical University, Chongqing 400016)
基金项目:Project supported by the Foundation for Foreign Scientists from the Ministry of Spanish Culture and Education (No. SB9751204311), the Personnel Department of China, the Sciences and Technology Committee of Chongqing.
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.


Structural Determination of Bis-histidinopeptide Zinc Complexes by 15N NMR (HMBC) Spectra
ZHOU,Cheng-He,Juan F.Miravet,M.Isabel Burguete,Santiago V.Luis,BAI,Xue,YUAN,Yong.Structural Determination of Bis-histidinopeptide Zinc Complexes by 15N NMR (HMBC) Spectra[J].Chinese Journal of Organic Chemistry,2004,24(Z1):380.
Authors:ZHOU  Cheng-He  Juan FMiravet  MIsabel Burguete  Santiago VLuis  BAI  Xue  YUAN  Yong
Abstract: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.
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