title: Measuring single small molecule binding via rupture forces of a split aptamer.
abstract: The rupture force of a split (bipartite) aptamer that forms binding pockets for adenosine monophosphate (AMP) was measured by atomic force spectroscopy. Changes in the rupture force were observed in the presence of AMP, while this effect was absent when mutant aptamers or inosine were used. Thus, changes in the rupture force were a direct consequence of specific binding of AMP to the split aptamer. The split aptamer concept allowed the detection of nonlabeled AMP and enabled us to determine the dissociation constant on a single-molecule level.
authors.affiliation: Max Planck Institute for Polymer Research, 55128 Mainz, Germany.
authors.forename: Thi-Huong
authors.initials: TH
authors.lastname: Nguyen
authors.forename: Lorenz Jan
authors.initials: LJ
authors.lastname: Steinbock
authors.forename: Hans-Jürgen
authors.initials: HJ
authors.lastname: Butt
authors.forename: Mark
authors.initials: M
authors.lastname: Helm
authors.forename: Rüdiger
authors.initials: R
authors.lastname: Berger
mesh_terms: D000249:Adenosine Monophosphate / Q000737:chemistry*; D052157:Aptamers, Nucleotide / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D011485:Protein Binding
chemical_list: D052157:Aptamers, Nucleotide; D000249:Adenosine Monophosphate