title: Effect of dendrimers on selected enzymes--Evaluation of nano carriers.
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.
authors.affiliation: Department of General Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Poland. Electronic address: maksion@biol.uni.lodz.pl.
authors.forename: Maksim
authors.initials: M
authors.lastname: Ionov
authors.affiliation: Institute of Biophysics and Cell Engineering of NASB, Minsk, Belarus.
authors.forename: Aliaksei
authors.initials: A
authors.lastname: Ihnatsyeu-Kachan
authors.affiliation: Laboratory of Microscopy Imaging and Advanced Biological Technics, University of Lodz, Poland.
authors.forename: Sylwia
authors.initials: S
authors.lastname: Michlewska
authors.affiliation: Republican Research and Practical Center of Neurology and Neurosurgery, Minsk, Belarus.
authors.forename: Natallia
authors.initials: N
authors.lastname: Shcharbina
authors.affiliation: Laboratory of Microscopy Imaging and Advanced Biological Technics, University of Lodz, Poland.
authors.forename: Dzmitry
authors.initials: D
authors.lastname: Shcharbin
authors.affiliation: Laboratorie de Chimie de Coordination, CNRS, Toulouse, France.
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Majoral
authors.affiliation: Department of General Biophysics, Faculty of Biology and Environmental Protection, University of Lodz, Poland.
authors.forename: Maria
authors.initials: M
authors.lastname: Bryszewska
mesh_terms: D000469:Alkaline Phosphatase / Q000378:metabolism; D001219:Aspartate Aminotransferases / Q000378:metabolism; D002412:Cations / Q000737:chemistry; D002942:Circular Dichroism; D050091:Dendrimers / Q000737:chemistry* / Q000378:metabolism; D004337:Drug Carriers / Q000737:chemistry* / Q000378:metabolism; D000067493:Dynamic Light Scattering; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D046529:Microscopy, Electron, Transmission; D036103:Nanotechnology / Q000379:methods*; D010455:Peptides / Q000378:metabolism; D010758:Phosphorus / Q000737:chemistry; D013050:Spectrometry, Fluorescence
chemical_list: D002412:Cations; D050091:Dendrimers; D004337:Drug Carriers; D010455:Peptides; D010758:Phosphorus; D007770:L-Lactate Dehydrogenase; D001219:Aspartate Aminotransferases; D000469:Alkaline Phosphatase
keywords: Complex formation; Phosphorus dendrimer; Plasma regulatory proteins; Surface charge