Figure 1.
Chemical structures of polyamines and PAMAM-G4 dendrimer.
Figure 2.
FTIR spectra and difference spectra (diff.) in the region of 1800-600 cm−1 of hydrated films (pH 7.4) for free mPEG-PAMAM-G3 (A), mPEG-PAMAM-G4 (B) PAMAM-G4 (C) (0.5 mM) and their spermine complexes obtained at different spermine concentrations (indicated on the figure).
Figure 3.
FTIR spectra and difference spectra (diff.) in the region of 1800-600 cm−1 of hydrated films (pH 7.4) for free mPEG-PAMAM-G3 (A), mPEG-PAMAM-G4 (B) PAMAM-G4 (C) (0.5 mM) and their spermidine complexes obtained at different spermidine concentrations (indicated on the figure).
Figure 4.
FTIR spectra and difference spectra (diff.) in the region of 1800-600 cm−1 of hydrated films (pH 7.4) for free mPEG-PAMAM-G3 (A), mPEG-PAMAM-G4 (B) PAMAM-G4 (C) (0.5 mM) and their BE-333 complexes obtained at different BE-333 concentrations (indicated on the figure).
Figure 5.
FTIR spectra and difference spectra (diff.) in the region of 1800-600 cm−1 of hydrated films (pH 7.4) for free mPEG-PAMAM-G3 (A), mPEG-PAMAM-G4 (B) PAMAM-G4 (C) (0.5 mM) and their BE-3333 complexes obtained at different BE-3333 concentrations (indicated on the figure).
Figure 6.
FTIR spectra in the region of 3300-2800 cm−1 of hydrated films (pH 7.4) for free mPEG-PAMAM-G3 (A), mPEG-PAMAM-G4 (B) and PAMAM-G4 (C) and their polyamine complexes obtained with 0.5 mM polymer and polyamine concentrations.
Figure 7.
UV-visible spectra of mPEG-PAMAM-G3, mPEG-PAMAM-G4 and PAMAM-G4 and their complexes with spermine and spermidine with free dendrimer at 100 µM and complexes c-g at 5, 10, 20, 40 and 80 µM.
(A, B and C) for spermine and c-g at 5, 10, 20, 40, and 80 µM for spermidine.mPEG-G3 (D), c-h c-g at 5, 10, 20, 40, 80 and 100 µM for spermidine-mPEG-G4 (E) and spermidine-PAMAM-G4 (F). Plots of 1/(A−A0) vs (1/ polyamine concentration) and binding constant ( K ) for spermine (A′, B′ and C′) and spermidine (D′, E′ and F′).
Figure 8.
UV-visible spectra of mPEG-PAMAM-G3, mPEG-PAMAM-G4 and PAMAM-G4 and their complexes with BE-333 and BE-3333 with free dendrimer at 100 µM and complexes c-h at 5, 10, 20, 40, 80 and 100 µM.
(A, B and C); c-h at 5, 10, 20, 40, 80 and 100 µM for BE-3333-mPEG-G3 (D), c-i at at 5, 10, 20, 40, 60, 80 and 100 µM BE-3333-mPEG-G4 (E) and c-f at 5, 10, 20 and 40 µM ( F). Plots of 1/(A−A0) vs (1/ polyamine concentration) and binding constant (K) for BE-333 (A′, B′ and C′) and BE-3333 (D′, E′ and F′).
Table 1.
Binding constants of polyamine-dendrimers (K M−1).
Figure 9.
Optimized polyamine-PAMAM-G4 docking structures.
The polyamines are shown in yellow color. (A) shows whole PAMAM-G4 in spheres with spermine and (A′) shows the zoom on the binding site represented in sticks. (B) shows whole PAMAM-G4 in spheres with spermidine and (B′) shows the binding site represented in sticks. (C) whole PAMAM-G4 in spheres with BE-333 and (C′) shows the binding site in represented in sticks.
Table 2.
Free binding energy of the docked polyamine-PAMAM complexes.