The interaction between PAMAM G3.5 dendrimer, Cd2+, dendrimer-Cd2+ complexes and human serum albumin.
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+.
Sekowski
Szymon
S
Department of General Biophysics, University of Lodz, Banacha 12/16, 90-237 Lodz, Poland. sekowski@biol.uni.lodz.pl
Kazmierczak
Andrzej
A
Mazur
Janusz
J
Przybyszewska
Magdalena
M
Zaborski
Marian
M
Shcharbin
Dzmitry
D
Gabryelak
Teresa
T
D002104:Cadmium / Q000378:metabolism*; D050091:Dendrimers / Q000378:metabolism*; D019075:Electrophoresis, Capillary; D005454:Fluorescence Polarization; D006801:Humans; D007700:Kinetics; D012709:Serum Albumin / Q000378:metabolism*; D012996:Solutions
D050091:Dendrimers; C522260:PAMAM G3.5 dendrimer; D012709:Serum Albumin; D012996:Solutions; D002104:Cadmium