Ontology highlight
ABSTRACT:
SUBMITTER: Neundlinger I
PROVIDER: S-EPMC3183820 | biostudies-other | 2011 Oct
REPOSITORIES: biostudies-other
Neundlinger Isabel I Poturnayova Alexandra A Karpisova Ivana I Rankl Christian C Hinterdorfer Peter P Snejdarkova Maja M Hianik Tibor T Ebner Andreas A
Biophysical journal 20111001 7
Thrombin aptamer binding strength and stability is dependent on sterical parameters when used for atomic force microscopy sensing applications. Sterical improvements on the linker chemistry were developed for high-affinity binding. For this we applied single molecule force spectroscopy using two enhanced biotinylated thrombin aptamers, BFF and BFA immobilized on the atomic force microscopy tip via streptavidin. BFF is a dimer composed of two single-stranded aptamers (aptabody) connected to each ...[more]