The unusual binding abilities of the His-analogue of Arg-vasopressin towards Cu2+.
A new vasopressin analogue, [His1,6]AVP, was synthesized and characterized by potentiometric measurements as well as by UV-Vis, CD and EPR spectroscopy. At the physiological pH the peptide forms a stable complex with Cu2+ ions which is characterized by the {NH2, NIm, NIm(macrochelate)} binding mode. The replacement of both Cys by His residues in the vasopressin sequence results in a very significant increase in the efficiency of Cu2+ binding.
Brasuń
Justyna
J
Department of Inorganic Chemistry, Wrocław Medical University, Szewska 38, 50-139, Wrocław, Poland. jbrasun@chnorg.am.wroc.pl
Cebrat
Marek
M
Sochacka
Aleksandra
A
Gładysz
Olimpia
O
Swiatek-Kozłowska
Jolanta
J
D001127:Arginine Vasopressin / Q000031:analogs & derivatives* / Q000737:chemistry*; D001665:Binding Sites; D003300:Copper / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D006639:Histidine / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D009942:Organometallic Compounds / Q000138:chemical synthesis / Q000737:chemistry*; D011199:Potentiometry
D008024:Ligands; D009942:Organometallic Compounds; D001127:Arginine Vasopressin; D006639:Histidine; D003300:Copper