Serum albumins have five sites for binding of cationic dendrimers.
The detailed analysis of the interaction between PAMAM G4 dendrimer and serum albumins was performed using circular dichroism, isothermal titration calorimetry, capillary electrophoresis, zeta-potential and fluorescence polarization. It was shown that serum albumins and PAMAM G4 dendrimer form the complex with stoichiometry of 4-6:1 for G4:HSA and 4-5:1 for G4:BSA molar ratio. The possible sites of PAMAM G4 dendrimers binding to protein surface were discussed. Also, it has been proposed that dendrimer does not significantly affect the protein secondary structure studied by circular dichroism.
Shcharbin
Dzmitry
D
Department of General Biophysics, University of Lodz, Banacha 12/16, 90-237 Lodz, Poland. shcharbi@biol.uni
Janicka
Magdalena
M
Wasiak
Michal
M
Palecz
Bartlomiej
B
Przybyszewska
Magdalena
M
Zaborski
Marian
M
Bryszewska
Maria
M
D000818:Animals; D001331:Automation; D001665:Binding Sites; D002412:Cations; D002417:Cattle; D002942:Circular Dichroism; D050091:Dendrimers; D019075:Electrophoresis, Capillary / Q000379:methods; D005454:Fluorescence Polarization; D008958:Models, Molecular; D008968:Molecular Conformation; D011073:Polyamines / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012709:Serum Albumin / Q000737:chemistry*
D002412:Cations; D050091:Dendrimers; C104700:PAMAM Starburst; D011073:Polyamines; D012709:Serum Albumin