0000000000331596

AUTHOR

Marek ŁUczkowski

0000-0002-5721-8380

showing 2 related works from this author

Binding abilities of dehydropeptides towards Cu(II) and Ni(II) ions. Impact of Z–E isomerization on metal ion binding

2002

The study on the binding ability of dehydro-tri- and tetrapeptides has shown that the alpha,beta-double bond has a critical effect on the peptide coordination to metal ions. It may affect the binding of the vicinal amide nitrogens by the electronic effect and stabilize the complex due to steric effects. The (Z) isomer is the most effective in stabilizing of the complexes formed. The presence of large side chain in the dehydroamino acid residue may also be critical for the coordination mode in the metallopeptide systems.

Steric effectsNickel(II) complexesE–Z isomersMetal ion bindingChemistryMetal ions in aqueous solutionPhotochemistryBiochemistryisomerizationInorganic ChemistryMetalCrystallographychemistry.chemical_compounddehydropeptidesAmidevisual_artSide chainvisual_art.visual_art_mediumElectronic effectCopper(II) complexesIsomerizationVicinalJournal of Inorganic Biochemistry : an interdisciplinary journal
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Structural analysis of copper(I) interaction with amyloid β peptide

2019

Abstract The N-terminal fragment of Aβ (β = beta) peptide is able to bind essential transition metal ions like, copper, zinc and iron. Metal binding usually occurs via the imidazole nitrogens of the three His residues which play a key role in the coordination chemistry. Among all the investigated systems, the interaction between copper and Amyloid β assume a biological relevance because of the interplay between the two copper oxidation states, Cu(II) and Cu(I), and their involvement in redox reactions. Both copper ions share the ability to bind Amyloid β. A huge number of investigations have demonstrated that Cu(II) anchors to the N-terminal amino and His6, His13/14 imidazole groups, while …

AmyloidSilverCoordination spherechemistry.chemical_elementPeptide010402 general chemistrySilver(I)01 natural sciencesBiochemistryRedoxCoordination complexInorganic ChemistryMetalchemistry.chemical_compoundCoordination ComplexesImidazoleHistidineAmino Acid SequenceHistidinechemistry.chemical_classificationAmyloid beta-Peptides010405 organic chemistryChemistryStructureCopperPeptide Fragments0104 chemical sciencesCrystallographyCoordinationvisual_artvisual_art.visual_art_mediumCopper(I)CopperProtein BindingJournal of Inorganic Biochemistry
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