The unusual coordination abilities of the peptides with betaXaaHisGlyHis sequence. The influence of structural modification of the peptide chain on the copper(II) binding.
The coordination abilities of tetrapeptides containing beta-amino acids towards Cu(II) ions are presented. The studied tetrapeptides were: Ac-betaAlaHisGlyHis, betaAlaHisGlyHis, Ac-betaAspHisGlyHis, betaAspHisGlyHis, Ac-betaAspHisGly-dHis and betaAspHisGly-dHis. Thorough potentiometric titrations were carried out to establish the stoichiometry of the resulting metal-ligand complexes and the role of free -alphaCOO(-) side chain group in metal binding. The copper(II) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV-Vis, EPR, CD) in strict correlation with potentiometric measurements.
Department of Inorganic Chemistry, Wrocław Medical University, Szewska 38, 50-139, Wrocław, Poland. jbrasun@chnorg.am.wroc.pl
Justyna
J
Brasuń
Hanna
H
Czapor
Agnieszka
A
Matera-Witkiewicz
Aleksandra
A
Kotynia
Aleksandra
A
Sochacka
Marek
M
Cebrat
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011485:Protein Binding; D055550:Protein Stability; D013056:Spectrophotometry, Ultraviolet
D010455:Peptides; D003300:Copper