effect of common buffers and heterocyclic ligands on the binding of cu(ii) at the multimetal binding site in human serum albumin常见的缓冲区和杂环配体对铜(ii)的绑定multimetal人类血清白蛋白结合位点.pdfVIP

Hindawi Publishing Corporation Bioinorganic Chemistry and Applications Volume 2010, Article ID 725153, 7 pages doi:10.1155/2010/725153 Research Article Effect of Common Buffers and Heterocyclic Ligands on the Binding of Cu(II) at the Multimetal Binding Site in Human Serum Albumin Magdalena Sokołowska,1 Krystyna Pawlas,1 and Wojciech Bal2, 3 1 Department of Hygiene, Wrocław Medical University, Mikulicza-Radeckiego 7, 50-345 Wrocław, Poland 2 Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warsaw, Poland ´ 3 Central Institute for Labour Protection-National Research Institute, Czerniakowska 16, 00-701 Warsaw, Poland Correspondence should be addressed to Wojciech Bal, wbal@ibb.waw.pl Received 16 December 2009; Accepted 16 February 2010 Academic Editor: Spyros Perlepes Copyright © 2010 Magdalena Sokołowska et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Visible-range circular dichroism titrations were used to study Cu(II) binding properties of Multimetal Binding Site (MBS) of Human Serum Albumin (HSA). The formation of ternary MBS-Cu(II)-Buffer complexes at pH 7.4 was positively verified for sodium phosphate, Tris, and Hepes, the three most common biochemical buffers. The phosphate Hepes Tris order of affinities, together with strong spectral changes induced specifically by Tris, indicates the presence of both Buffer-Cu(II) and Buffer-HSA interactions. All complexes are strong enough to yield a nearly 100% ternary complex formation in 0.5 mM HSA dissolved in 10