Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1178387 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2007 | 6 Pages |
Abstract
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Dzmitry Shcharbin, Magdalena Janicka, Michal Wasiak, Bartlomiej Palecz, Magdalena Przybyszewska, Marian Zaborski, Maria Bryszewska,