title: Short peptides are not reliable models of thermodynamic and kinetic properties of the N-terminal metal binding site in serum albumin.
abstract: A comparative study of thermodynamic and kinetic aspects of Cu(II) and Ni(II) binding at the N-terminal binding site of human and bovine serum albumins (HSA and BSA, respectively) and short peptide analogues was performed using potentiometry and spectroscopic techniques. It was found that while qualitative aspects of interaction (spectra and structures of complexes, order of reactions) could be reproduced, the quantitative parameters (stability and rate constants) could not. The N-terminal site in HSA is much more similar to BSA than to short peptides reproducing the HSA sequence. A very strong influence of phosphate ions on the kinetics of Ni(II) interaction was found. This study demonstrates the limitations of short peptide modelling of Cu(II) and Ni(II) transport by albumins.
authors.affiliation: Faculty of Chemistry, University of Wroclaw, Poland.
authors.forename: Magdalena
authors.initials: M
authors.lastname: Sokolowska
authors.forename: Artur
authors.initials: A
authors.lastname: Krezel
authors.forename: Marcin
authors.initials: M
authors.lastname: Dyba
authors.forename: Zbigniew
authors.initials: Z
authors.lastname: Szewczuk
authors.forename: Wojciech
authors.initials: W
authors.lastname: Bal
mesh_terms: D000818:Animals; D016477:Artifacts; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D002417:Cattle; D003300:Copper / Q000378:metabolism*; D006801:Humans; D008956:Models, Chemical; D009532:Nickel / Q000378:metabolism*; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism*; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism; D013045:Species Specificity; D013816:Thermodynamics
chemical_list: D002352:Carrier Proteins; D009842:Oligopeptides; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; D003300:Copper; D009532:Nickel