The interaction between PAMAM G3.5 dendrimer, Cd2+, dendrimer-Cd2+ complexes and human serum albumin.

Abstract

The interactions between PAMAM G3.5 dendrimer, Cd2+, a complex of "PAMAM G3.5 dendrimer-Cd2+" and human serum albumin were studied by equilibrium dialysis, fluorescence quenching, fluorescence anisotropy and zeta-potential. It was found that in water one molecule of PAMAM 3.5 dendrimer can bind 38+/-9 cadmium ions with Kb=1.3+/-0.13 x 10(3). The calculated Stern-Volmer constants of albumin fluorescence quenching by Cd2+, G3.5 and the "PAMAM G3.5-Cd2+" complex were 2.2+/-0.2, 1.6+/-0.3 and 1.4+/-0.1(mmol/l)(-1), respectively. The data from the fluorescence and zeta-potential studies show that the "PAMAM G3.5-Cd2+" complex interacted much less strongly with human serum albumin than the pure dendrimer or Cd2+.

DOI: 10.1016/j.colsurfb.2008.11.006

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Cite this paper

@article{Sekowski2009TheIB, title={The interaction between PAMAM G3.5 dendrimer, Cd2+, dendrimer-Cd2+ complexes and human serum albumin.}, author={Szymon Sekowski and Andrzej Kaźmierczak and Janusz Mazur and Magdalena Przybyszewska and Marian Zaborski and Dzmitry Shcharbin and Teresa Gabryelak}, journal={Colloids and surfaces. B, Biointerfaces}, year={2009}, volume={69 1}, pages={95-8} }