Wyniki wyszukiwania - BazTech

Ograniczanie wyników

2 Wiadomości Chemiczne

Znaleziono wyników: 2

Liczba wyników na stronie

Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych: reszta histydylowa

Sortuj według:

Ogranicz wyniki do:

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.

Peptydy jako potencjalne ligandy wiążące jony metali przejściowych

Krupa K., Lesiów M. K., Kowalik-Jankowska T.

Wiadomości Chemiczne

2018

[Z] 72, 7-8

597--608

Peptides are crucial ligands for transition metal ions and form complexes with them, that can have important biological activity. Many factors impact on the creation of complexes such as: protection of amine group from N-terminal or carboxylate group from C-terminals of the protein, the presence of noncoordinating and coordinating side chains in the peptide sequence, the number of histidyl residues and their location in the peptide chain. In complexes the metal ion can be bound bound by various donor atoms from amino acids residues (e.g. nitrogen, oxygen or sulphur). In general, the protection of N- or C-terminal groups influences the less stable formation of complexes. Stable complexes are created, if the free amine group from the N-terminal is involved in the coordination process. Peptides with noncoordinating side chains include alanine or glycine. Glycine complexes are more stable than these with alanine. Histidyl residue is the most effective amino acid residue in binding metal ions. The amine group of the lysyl residue, thiol from cysteine or carboxylate from aspartyl or glutamyl residues are also functional groups that coordinate metal ions. The coordination process is initiated by a group that anchors metal ion. A free amine group from N-terminus or imidazole nitrogen are the best examples of anchor groups. The metal ions can also be bound through amide nitrogens, after their forced deprotonation by the anchor group and formation of chelate rings. Peptides containing two or more histidyl residues exhibit high structural diversity in the complexes formation. In addition, these peptides can also form macrochelates and polynuclear complexes. The location of amino acid residues in the peptide chain (especially histydyl residue) also results in the thermodynamically stable formation of complexes.