4.7 Article

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

Journal

COLLOIDS AND SURFACES B-BIOINTERFACES
Volume 69, Issue 1, Pages 95-98

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.colsurfb.2008.11.006

Keywords

PAMAM 3.5 dendrimer; Human serum albumin; Cadmium ions; Dendrimer-cadmium complex

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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 K-b = 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+. (c) 2008 Elsevier B.V. All rights reserved.

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