6533b82afe1ef96bd128c377

RESEARCH PRODUCT

Measuring single small molecule binding via rupture forces of a split aptamer.

Lorenz J. SteinbockMark HelmRüdiger BergerThi-huong NguyenHans-jürgen Butt

subject

Adenosine monophosphateChemistryAptamerForce spectroscopyGeneral ChemistryPlasma protein bindingAptamers NucleotideMicroscopy Atomic ForceBiochemistryCatalysisAdenosine MonophosphateDissociation constantCrystallographychemistry.chemical_compoundColloid and Surface ChemistrymedicineDirect consequenceSmall molecule bindingInosinemedicine.drugProtein Binding

description

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.

yearjournalcountryeditionlanguage
2011-02-02Journal of the American Chemical Society
10.1021/ja1092002https://pubmed.ncbi.nlm.nih.gov/21287983