Abstract
In the field of nanotechnology, dendrimers represent a new class of highly branched macromolecules that is receiving a stimulating and rising interest. The structural organization of these synthetic macromolecules provides promising opportunities for using them as nano-carriers of drugs or gene material to be delivered to the target cells. For applications of dendrimers as drug carriers, analysis of their specific interactions with biological structures at molecular level is very important. This paper describes the molecular interactions between cationic phosphorus dendrimers of third and fourth generation (CPD G3 and CPD G4) and 3 plasma regulatory proteins, namely aspartate transaminase, alkaline phosphatase and l-lactic dehydrogenase. Dendrimer–protein interactions were studied using spectrofluorimetric, circular dichroism and dynamic light scattering techniques. Their morphology in the presence or absence of dendrimers was examined by transmission electron microscopy. The results suggest that both dendrimers form positively charged complexes with HIV-derived peptides. The circular dichroism spectra show that these dendrimers can significantly change the secondary structure of proteins, indicating formation of protein/dendrimer complexes.
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