title: Giant Host Red Blood Cell Membrane Mimicking Polymersomes Bind Parasite Proteins and Malaria Parasites.
abstract: Malaria is an infectious disease that needs to be addressed using innovative approaches to counteract spread of drug resistance and to establish or optimize vaccination strategies. With our approach, we aim for a dual action with drug- and 'vaccine-like' activity against malaria. By inhibiting entry of malaria parasites into host red blood cells (RBCs) - using polymer vesicle-based (polymersome) nanomimics of RBC membranes - the life cycle of the parasite is interrupted and the exposed parasites are accessible to the host immune system. Here, we describe how host cell-sized RBC membrane mimics, formed with the same block copolymers as nanomimics, also bind the corresponding malaria parasite ligand and whole malaria parasites, similar to nanomimics. This was demonstrated using fluorescence imaging techniques and confirms the suitability of giant polymersomes (GUVs) as simple mimics for RBC membranes.
authors.affiliation: Department of Chemistry, University of Basel, Klingelbergstrasse 80 CH-4056, Switzerland; Swiss Tropical and Public Health Institute, Socinstrasse 57 Postfach, CH-4002, Switzerlandl; University of Basel, Petersgraben 2, CH-4002 Basel, Switzerland.
authors.forename: Adrian
authors.initials: A
authors.lastname: Najer
authors.affiliation: Department of Chemistry, University of Basel, Klingelbergstrasse 80, CH-4056 Basel, Switzerland.
authors.forename: Sagana
authors.initials: S
authors.lastname: Thamboo
authors.affiliation: Department of Chemistry, University of Basel, Klingelbergstrasse 80, CH-4056 Basel, Switzerland.
authors.forename: Cornelia G
authors.initials: CG
authors.lastname: Palivan
authors.affiliation: Swiss Tropical and Public Health Institute, Socinstrasse 57 Postfach, CH-4002, Switzerland; University of Basel, Petersgraben 2, CH-4002 Basel, Switzerland.
authors.forename: Hans-Peter
authors.initials: HP
authors.lastname: Beck
authors.affiliation: Department of Chemistry, University of Basel, Klingelbergstrasse 80, CH-4056 Basel, Switzerland. wolfgang.meier@unibas.ch.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Meier
mesh_terms: D000962:Antimalarials / Q000138:chemical synthesis / Q000378:metabolism*; D040761:Biomimetic Materials / Q000138:chemical synthesis / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000737:chemistry; D006493:Heparin / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D020066:Merozoite Surface Protein 1 / Q000737:chemistry / Q000378:metabolism*; D052940:Merozoites / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D010080:Oxazoles / Q000138:chemical synthesis*; D010963:Plasmodium falciparum / Q000378:metabolism*; D011108:Polymers / Q000138:chemical synthesis*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D053835:Unilamellar Liposomes / Q000138:chemical synthesis / Q000378:metabolism
chemical_list: D000962:Antimalarials; D020066:Merozoite Surface Protein 1; D010080:Oxazoles; D011108:Polymers; D011994:Recombinant Proteins; D053835:Unilamellar Liposomes; C542789:poly(2-methyl oxazoline)-block polydimethylsiloxane-block-poly(2-methyl oxazoline); D006493:Heparin