Understanding the binding interactions between dendrimer and 18 common amino acids by NMR techniques.

In the present study, we focus on the interactions between poly(propylene imine) (PPI) dendrimer and 18 of the 20 common amino acids by several NMR techniques, including NMR titrations and NOESY analysis. Surface ionic interactions and interior encapsulations were observed, and the binding behavior of amino acids with PPI dendrimer depends much on the side-chain properties of the amino acid, such as charge and hydrophobic/hydrophilic properties. The (1)H NMR titration results show that the formation of PPI dendrimer-amino acid complexes are driven mainly by ionic interactions for all the amino acids except tryptophan, which is involved in strong hydrophobic interactions with the interior pockets of PPI. The hydrophobic encapsulation of tryptophan in PPI pockets is confirmed by NOESY analysis. Amino acids with negatively charged residues much more easily saturate the surface charges on PPI than amino acids with uncharged residues, whereas amino acids with positively charged residues are the most difficult to bind with the surface amine groups on the PPI dendrimer. A simultaneous occurrence of interior encapsulation (hydrophobic, hydrogen bond, or ionic interactions) and surface binding (ionic interactions) was observed for tryptophan, phenylalanine, arginine, lysine, histidine, cysteine, and asparagine, and a preferential surface ionic binding on the PPI surface rather than encapsulations in the interior was obtained for the other amino acids.