title: Effect of functionalization of carbon nanotubes with psychosine on complement activation and protein adsorption.
abstract: Carbon nanotubes possess interesting physicochemical properties which make them potentially usable in medicine. Single-walled carbon nanotubes and multi-walled carbon nanotubes, for example, may carry and deliver anticancer drugs, such as cisplatin. Magnetic nanoparticles, like iron filled MWCNT, can be used in hyperthermia therapy. However, their hydrophobic character is a major difficulty, as preparation of stable dispersions of carbon nanotubes in biological buffers is an essential step towards biomedical applications. Recently, a novel treatment using the glycolipid, Galactosyl-beta1-sphingosine (psychosine), was employed to make stable suspensions of psychosine-functionalized carbon nanotubes in biological buffers. In this paper, the interactions of psychosine-functionalized carbon nanotubes with a part of the human immune system, complement, is presented. To investigate if human serum complement proteins can interact with psychosine-functionalized carbon nanotubes, complement consumption (depletion) assays were conducted. Moreover, direct protein binding studies, to analyze the interaction of plasma proteins with the psychosine-functionalized carbon nanotubes, using affinity chromatography and sodium dodecyl sulphate polyacrylamide gel electrophoresis techniques, were applied. The psychosine-functionalized carbon nanotubes activate human complement via the classical pathway. Interestingly, as the hydrophilic part of the glycolipid may bind to ficolins, the lectin pathway could also be involved. Binding of human plasma proteins is very selective as only very few proteins adsorb to the psychosine-functionalized carbon nanotube surface, when placed in contact with human plasma. Bovine serum albumin-coated carbon nanotubes were used as a standard to find the differences in complement activation and protein adsorption patterns, caused by various non-covalent coatings of carbon nanotubes.
authors.affiliation: Department of Pharmacology, University of Oxford, Mansfield Road, Oxford OX1 3QT7 United Kingdom.
authors.forename: Malgorzata J
authors.initials: MJ
authors.lastname: Rybak-Smith
authors.forename: Carla
authors.initials: C
authors.lastname: Tripisciano
authors.forename: Ewa
authors.initials: E
authors.lastname: Borowiak-Palen
authors.forename: Constanze
authors.initials: C
authors.lastname: Lamprecht
authors.forename: Robert B
authors.initials: RB
authors.lastname: Sim
mesh_terms: D000327:Adsorption / Q000187:drug effects; D000818:Animals; D001798:Blood Proteins / Q000378:metabolism; D002417:Cattle; D003167:Complement Activation / Q000187:drug effects*; D003165:Complement System Proteins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D013058:Mass Spectrometry; D018625:Microscopy, Atomic Force; D037742:Nanotubes, Carbon / Q000737:chemistry*; D011485:Protein Binding / Q000187:drug effects; D011609:Psychosine / Q000737:chemistry / Q000494:pharmacology*; D012710:Serum Albumin, Bovine / Q000378:metabolism
chemical_list: D001798:Blood Proteins; D037742:Nanotubes, Carbon; D011609:Psychosine; D012710:Serum Albumin, Bovine; D003165:Complement System Proteins