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Australian Journal of Chemistry Australian Journal of Chemistry Society
An international journal for chemical science
RESEARCH ARTICLE

New Method for the Synthesis of a Mononucleating Cyclic Peptide Ligand, Crystal Structures of its Ni, Zn, Cu, and Co Complexes, and Their Inhibitory Bioactivity Against Urease

Kui Cheng A B , Zhong-Lu You A B and Hai-Liang Zhu A B C
+ Author Affiliations
- Author Affiliations

A Institute of Functional Biomolecules, State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, China.

B School of Chemical Engineering, Wuhan University of Science and Engineering, Wuhan 430073, China.

C Corresponding author. Email: zhuhl@nju.edu.cn

Australian Journal of Chemistry 60(5) 375-379 https://doi.org/10.1071/CH06479
Submitted: 18 December 2006  Accepted: 5 April 2007   Published: 28 May 2007

Abstract

A novel cyclic peptide complex, NiL 1 (H2L = 12,24-dihydroxy-1,6-dioxo-2,5,14,17-tetraaza[6*6]metacyclophane-13,17-diene has been synthesized for the first time under solvothermal conditions through a one-pot synthetic procedure using nickel ion as the template reagent. It was found that other metal ions were not suitable for the direct template reagent in this reaction. The nickel ion was eliminated from the complex and the metal-free cyclic peptide ligand H2L was obtained through a series of reactions. Then, ZnII, CuII, and CoII were coordinated with H2L under the same solvothermal conditions to produce three isomorphous complexes ZnL 2, CuL 3, and CoL 4. Their inhibitory bioactivities against urease were then studied. The copper(ii) complex 3 was the strongest inhibitor against jack bean urease, while H2L, 2, and 4 showed weak or no inhibitory activity against this enzyme.


Acknowledgments

The work was financed by a grant (project 30672516) from the National Natural Science Foundation of China.


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