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1 2020

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Kompleksy peptydów z jonami Cu2+ jako mimetyki dysmutazy ponadtlenkowej

Pieniężna Aleksandra, Kotynia Aleksandra

Wiadomości Chemiczne

2020

[Z] 74, 11-12

735--759

Disturbances in the balance between the rates of reactive oxygen species formation and the ability of cells to neutralize them are often cause dysfunction in the human body. Therefore the research on natural antioxidant systems protecting cells against destruction is very important. One of such system acting in human organism is superoxide dismutase (SOD), which is responsible for degradation of the superoxide radical anion into molecular oxygen and hydrogen peroxide. The SOD was discovered in the 40s of the twentieth century, and since then there has been a lot of research on it. Currently, these studies mainly concern searching compounds that may mimic the enzymatic activity of this protein. Groups of these compounds include, for example, peptides, salens, metalloporphyrins or vitamin derivatives. For the proper functioning of the CuZnSOD enzyme necessary is the active center containing metal ions (Rys.2). They mainly coordinate to the nitrogens of the imidazole histidine residues. Due to the fact that peptides may have many histidyl residues in their structure, they could rather than others coordinate with metal ions and they are promising compounds in studies on CuZnSOD mimetics. Therefore we will consider peptide complexes with copper(II) and zinc(II) ions as potential mimetics of superoxide dismutase. In presented review article we have focused on the differences in the coordination manner of divalent copper ions by linear, cyclic and branched peptides. As well as the possibility of creating hetero- and homo-dinuclear complexes are discussed. Moreover we have compared the ability of these complexes to decomposition the superoxide radical with activity of native enzyme.