title: Following aptamer-ricin specific binding by single molecule recognition and force spectroscopy measurements.
abstract: Single molecule recognition imaging and dynamic force spectroscopy (DFS) analysis showed strong binding affinity between an aptamer and ricin, which was comparable with antibody-ricin interaction. Molecular simulation showed a ricin binding conformation with aptamers and gave different ricin conformations immobilizing on substrates that were consistent with AFM images.
authors.affiliation: Single Molecule Study Laboratory, Faculty of Engineering and Nanoscale Science and Engineering Center, University of Georgia, Athens, GA 30602, USA.
authors.forename: Bin
authors.initials: B
authors.lastname: Wang
authors.forename: Cunlan
authors.initials: C
authors.lastname: Guo
authors.forename: Guojun
authors.initials: G
authors.lastname: Chen
authors.forename: Bosoon
authors.initials: B
authors.lastname: Park
authors.forename: Bingqian
authors.initials: B
authors.lastname: Xu
mesh_terms: D052157:Aptamers, Nucleotide / Q000737:chemistry*; D001665:Binding Sites; D006046:Gold / Q000737:chemistry; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D012276:Ricin / Q000737:chemistry*
chemical_list: D052157:Aptamers, Nucleotide; D006046:Gold; D012276:Ricin