TY  - JOUR
AB  - Changes in the elastic properties of single deoxyribonucleic acid (DNA) molecules in the presence of different DNA-binding agents are identified using atomic force microscope single molecule force spectroscopy. We investigated the binding of poly(dG-dC) dsDNA with the minor groove binder distamycin A, two supposed major groove binders, an alpha-helical and a 3(10)-helical peptide, the intercalants daunomycin, ethidium bromide and YO, and the bis-intercalant YOYO. Characteristic mechanical fingerprints in the overstretching behavior of the studied single DNA-ligand complexes were observed allowing the distinction between different binding modes. Docking of ligands to the minor or major groove of DNA has the effect that the intramolecular B-S transition remains visible as a distinct plateau in the force-extension trace. By contrast, intercalation of small molecules into the double helix is characterized by the vanishing of the B-S plateau. These findings lead to the conclusion that atomic force microscope force spectroscopy can be regarded as a single molecule biosensor and is a potent tool for the characterization of binding motives of small ligands to DNA.
DA  - 2003
DO  - 10.1016/S0006-3495(03)74624-4
LA  - eng
IS  - 3
M2  - 1968
PY  - 2003
SN  - 0006-3495
SP  - 1968-1973
T2  - Biophysical journal
TI  - Identification of binding mechanisms in single molecule-DNA complexes
UR  - https://nbn-resolving.org/urn:nbn:de:0070-pub-16104364
Y2  - 2024-11-21T17:20:32
ER  -