title: The unusual binding abilities of the His-analogue of Arg-vasopressin towards Cu2+.
abstract: 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.
authors.affiliation: Department of Inorganic Chemistry, Wrocław Medical University, Szewska 38, 50-139, Wrocław, Poland. jbrasun@chnorg.am.wroc.pl
authors.forename: Justyna
authors.initials: J
authors.lastname: Brasuń
authors.forename: Marek
authors.initials: M
authors.lastname: Cebrat
authors.forename: Aleksandra
authors.initials: A
authors.lastname: Sochacka
authors.forename: Olimpia
authors.initials: O
authors.lastname: Gładysz
authors.forename: Jolanta
authors.initials: J
authors.lastname: Swiatek-Kozłowska
mesh_terms: 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
chemical_list: D008024:Ligands; D009942:Organometallic Compounds; D001127:Arginine Vasopressin; D006639:Histidine; D003300:Copper