6533b7d1fe1ef96bd125d821

RESEARCH PRODUCT

Influence of the position of two dehydro-amino acids residues in the oligopeptide sequence on the binding ability towards Cu(II) ions

Jolanta Swiatek-kozlowskaAnna JanickaMaciej MakowskiJustyna Brasuń

subject

chemistry.chemical_classificationOligopeptideStereochemistrySequence (biology)IonAmino acidInorganic ChemistryMetalchemistry.chemical_compoundBinding abilityCopper(II)Peptide backbonechemistryAmidevisual_artMaterials Chemistryvisual_art.visual_art_mediumdehydro-peptidesOrganic chemistryPhysical and Theoretical Chemistrycomplex

description

Abstract Studies on the binding ability of bis-dehydro-hexa- and pentapeptides have shown that the hexapeptides bind Cu+2 with similar efficacy as pentapeptides. The increase of distance between two dehydro-amino acid residues in the peptide backbone has no impact on the efficacy in metal ion binding. The type of isomeration [(Z) or (E)] has an influence on the coordination of the metal ion only to the first amide nitrogen.

yearjournalcountryeditionlanguage
2005-10-01Polyhedron
https://doi.org/10.1016/j.poly.2005.05.016