Dynamic Force Spectroscopy of the BabA–Lewis b Binding

Oscar Björnham , Jeanna Bugaytsova , Thomas Borén , Staffan Schedin

The binding strength of the adhesin–receptor complex BabA-ABO/Lewis b has been analyzed by means of Dynamic Force Spectroscopy. High‑resolution measurements of rupture forces were performed on single bacterial cells, expressing the high affinity binding BabA adhesin, by use of a force measuring optical tweezers. The resulting force spectra revealed the mechanical properties of a single BabA‑Leb bond. It was found that the bond is dominated by one single energy barrier and that it is a slip‑bond. The bond length and thermal off–rate were assessed to 0.86±0.07 nm and 0.015±0.006 s, respectively.

Mots clés: Optical tweezers; Single bond dissociation; Receptor–ligand interaction; Bond strength; Lewis b receptor

Oscar Björnham, Jeanna Bugaytsova, Thomas Borén, Staffan Schedin. Dynamic Force Spectroscopy of the BabA–Lewis b Binding. Biophysical Chemistry, 2009, 143 (1-2), pp.102. ⟨10.1016/j.bpc.2009.03.007⟩. ⟨hal-00540533⟩