Abstract

Dendrimers are hyperbranched polymers belonging to the class of nanomaterials. These nanostructures and their derivatives (dendrons and dendronized nanoparticles) are multi-target nanocarriers that can be modified to achieve various tasks. For example, it is possible to increase biocompatibility and stability, to control the release of active substances. Their widespread use in biology and medicine requires an understanding of the basic mechanisms of their interaction with proteins - one of the main biological systems. The interaction of dendrimers with proteins may vary depending on the size of the ones, surface charge, structure and stiffness of the branches. Here, both electrostatic interactions arising due to the presence of dendrimers and surface charge proteins, as well as hydrophobic ones, due to the corresponding cavities in the structure of dendrimers, can manifest themselves here. The formation of hydrogen bonds is possible. All these interactions in one way or another can affect the structure and functions of proteins. Present article discusses the mechanisms of interactions between dendrimers, dendronized nanoparticles and protein macromolecules. The effect of nanoparticles on the secondary structure, conformation, dynamics and functional activity of proteins is reviewed. The different models for dendrimer-protein interactions are described.

Highlights

  • Dendrimers are hyperbranched polymers belonging to the class of nanomaterials

  • It is possible to increase biocompatibility and stability, to control the release of active substances. Their widespread use in biology and medicine requires an understanding of the basic mechanisms of their interaction with proteins – one of the main biological systems

  • The interaction of dendrimers with proteins may vary depending on the size of the ones, surface charge, structure and stiffness of the branches

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Summary

22. Lactose-containing starburst dendrimers

Influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties / S. Dendrimers bind human serum albumin / E. Dendrimers destabilize proteins in a generation-dependent manner involving electrostatic interactions / L. PAMAM G4 dendrimers as inhibitors of the iron storage properties of human L-chain ferritin / M. Dendrimer-protein interactions studied by tryptophan room temperature phosphorescence / E. Impact of PAMAM G2 and G6 dendrimers on bovine serum albumin (fatty acids free and loaded with different fatty acids) / D. Stabilizing effect of small concentrations of PAMAM dendrimers at the insulin aggregation / O. Nowacka [et al.] // Colloids Surfaces B Biointerfaces. Shcharbin [et al.] // Colloids Surfaces B: Biointerfaces.

34. Nanoparticle corona for proteins
44. Therapeutic benefits from nanoparticles

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