Dendrimer-protein interactions versus dendrimer-based nanomedicine
Creators
- 1. Institute of Biophysics and Cell Engineering of NASB, Minsk, Belarus
- 2. Clinics at the MAZ Company, Minsk, Belarus
- 3. nstitute of Biophysics and Cell Engineering of NASB, Minsk, Belarus
- 4. Department of General Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland
- 5. Université Paris Descartes, Laboratoire de Chimie et de Biochimie pharmacologiques et toxicologique, Paris, France
- 6. Departamento Química Orgánica y Química Inorgánica, Universidad de Alcalá, Alcalá de Henares, Spain; Networking Research Center on Bioengineering, Biomaterials and Nanomedicine, CIBER-BBN, Spain
- 7. Networking Research Center on Bioengineering, Biomaterials and Nanomedicine, CIBER-BBN, Spain; Laboratorio InmunoBiología Molecular, Hospital General Universitario Gregorio Marañón, Madrid, Spain; Instituto de Investigación Sanitaria Gregorio Marañón (IiSGM), Madrid, Spain; Spanish HIV-HGM BioBank, Madrid, Spain
- 8. aboratoire de Chimie de Coordination, CNRS, Toulouse, France ; Université de Toulouse, Toulouse, France
Description
Abstract
Dendrimers are hyperbranched polymers belonging to the huge class of nanomedical devices. Their wide application in biology and medicine requires understanding of the fundamental mechanisms of their interactions with biological systems. Summarizing, electrostatic force plays the predominant role in dendrimer-protein interactions, especially with charged dendrimers. Other kinds of interactions have been proven, such as H-bonding, van der Waals forces, and even hydrophobic interactions. These interactions depend on the characteristics of both participants: flexibility and surface charge of a dendrimer, rigidity of protein structure and the localization of charged amino acids at its surface. pH and ionic strength of solutions can significantly modulate interactions. Ligands and cofactors attached to a protein can also change dendrimer-protein interactions. Binding of dendrimers to a protein can change its secondary structure, conformation, intramolecular mobility and functional activity. However, this strongly depends on rigidity versus flexibility of a protein’s structure. In addition, the potential applications of dendrimers to nanomedicine are reviwed related to dendrimer-protein interactions.
Files
Dendrimer-protein interactions versus dendrimer-based nanomedicine.pdf
Files
(1.8 MB)
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