Sokolowska Magdalena, Krezel Artur, Dyba Marcin, Szewczuk Zbigniew, Bal Wojciech
Faculty of Chemistry, University of Wroclaw, Poland.
Eur J Biochem. 2002 Feb;269(4):1323-31. doi: 10.1046/j.1432-1033.2002.02772.x.
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.
采用电位滴定法和光谱技术，对铜（II）和镍（II）与人血清白蛋白（HSA）和牛血清白蛋白（BSA）的N端结合位点以及短肽类似物结合的热力学和动力学方面进行了比较研究。结果发现，虽然相互作用的定性方面（配合物的光谱和结构、反应顺序）可以重现，但定量参数（稳定性和速率常数）却无法重现。HSA中的N端位点与BSA的相似性远高于与重现HSA序列的短肽的相似性。研究发现磷酸根离子对镍（II）相互作用的动力学有非常强烈的影响。这项研究证明了用短肽模拟白蛋白转运铜（II）和镍（II）的局限性。
