Coordination Chemistry Approaches to Biological Activity Modulation: Copper Complexes and Enzyme Interactions
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Abstract
Coordination chemistry has emerged as a powerful approach for modulating biological activity through the design and application of metal complexes that interact with enzymatic systems. Copper complexes, in particular, have demonstrated significant potential in biological applications due to their unique redox properties, versatile coordination geometries, and ability to participate in electron transfer processes essential for enzymatic function. This review examines the fundamental principles underlying copper-enzyme interactions, focusing on the mechanisms by which synthetic copper complexes can modulate enzyme activity through coordination chemistry approaches. The investigation encompasses the structural characteristics of copper active sites in biological systems, the design strategies for artificial metalloproteins, and the therapeutic applications of copper complexes as enzyme inhibitors and modulators. Recent advances in multicopper oxidases, urease inhibition, and anticancer applications demonstrate the versatility of coordination chemistry in developing biologically active compounds. The study reveals that copper complexes can serve as both enzyme mimics and inhibitors, depending on their structural features and coordination environment. Understanding these interactions provides valuable insights for the rational design of next-generation therapeutic agents and the development of biomimetic catalysts with enhanced selectivity and efficiency for targeted biological applications.
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