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Poly(propylene imine) dendrimers can bind to PEGylated albumin at PEG and albumin surface: Biophysical examination of a PEGylated platform to transport cationic dendritic nanoparticles.
- Source :
-
Biopolymers [Biopolymers] 2020 Sep; Vol. 111 (9), pp. e23386. Date of Electronic Publication: 2020 Jun 16. - Publication Year :
- 2020
-
Abstract
- Cationic dendrimers are considered one of the best drug transporters in the body. However, in order to improve their biocompatibility, modification of them is required to reduce toxicity. In this way, many dendrimers may lose their original properties, for example, anticancer. To improve biocompatibility of dendrimers, it is possible to complex them with albumin, as is done very often in drug delivery. However, the interaction of dendrimers with albumin can lead to protein structure disruption or no complexation at all. Therefore, the investigation of the interaction between cationic poly-(propylene imine) dendrimers and polyethylene glycol (PEG)-albumin by fluorescence, circular dichroism, small angle X-ray scattering (SAXS), and transmission electron microscopy was carried out. Results show that cationic dendrimers bind to PEGylated albumin at PEG and albumin surfaces. The obtained results for 5k-PEG indicate a preferential binding of the dendrimers to PEG. For 20k-PEG binding of dendrimers to PEG and protein could induce a collapse of the PEG chain onto the protein surface. This opens up new possibilities to the use of PEGylated albumin as a platform to carry dendrimers without changing the albumin structure and improve the pharmacokinetic properties of dendrimers without further modification.<br /> (© 2020 Wiley Periodicals, Inc.)
- Subjects :
- Animals
Biological Transport
Cattle
Dendrimers metabolism
Drug Delivery Systems methods
Nanoparticles metabolism
Polyethylene Glycols metabolism
Polypropylenes metabolism
Scattering, Small Angle
Serum Albumin, Bovine metabolism
Surface Properties
X-Ray Diffraction
Dendrimers chemistry
Nanoparticles chemistry
Polyethylene Glycols chemistry
Polypropylenes chemistry
Serum Albumin, Bovine chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1097-0282
- Volume :
- 111
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Biopolymers
- Publication Type :
- Academic Journal
- Accession number :
- 32544981
- Full Text :
- https://doi.org/10.1002/bip.23386