title: Development and characterization of an aptamer binding ligand of fractalkine using domain targeted SELEX.
abstract: Fractalkine (FKN) is a unique cell surface protein with potential as a therapeutic target because of its role in inflammatory diseases and cancer. We developed an aptamer, named FKN-S2, with a dissociation constant of 3.4 ± 0.7 nM that is specific to the chemokine domain of fractalkine.
authors.affiliation: Department of Chemical Engineering and Materials Science, University of Minnesota, Minneapolis, MN 55455, USA.
authors.forename: Brett
authors.initials: B
authors.lastname: Waybrant
authors.forename: Timothy R
authors.initials: TR
authors.lastname: Pearce
authors.forename: Ping
authors.initials: P
authors.lastname: Wang
authors.forename: Srinand
authors.initials: S
authors.lastname: Sreevatsan
authors.forename: Efrosini
authors.initials: E
authors.lastname: Kokkoli
mesh_terms: D000818:Animals; D052157:Aptamers, Nucleotide / Q000737:chemistry / Q000378:metabolism*; D001483:Base Sequence; D001667:Binding, Competitive; D002417:Cattle; D054428:Chemokine CX3CL1 / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D052156:SELEX Aptamer Technique; D012710:Serum Albumin, Bovine / Q000378:metabolism
chemical_list: D052157:Aptamers, Nucleotide; D054428:Chemokine CX3CL1; D008024:Ligands; D012710:Serum Albumin, Bovine