Dynamic force spectroscopy of the Helicobacter pylori BabA-Lewis b binding
2009 (English)In: Biophysical Chemistry, ISSN 0301-4622, E-ISSN 1873-4200, Vol. 143, no 1-2, 102-105 p.Article in journal (Refereed) Published
The binding strength of the Helicobacter pylori adhesin–receptor complex BabA-ABO/Lewis b has been analyzed by means of dynamic force pectroscopy. High-resolution measurements of rupture forces were performed in situ on single bacterial cells, expressing the high-affinity binding BabA adhesin, by the use of 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 slipbond. The bond length and thermal off-rate were assessed to be 0.86±0.07 nm and 0.015±0.006 s−1, respectively.
Place, publisher, year, edition, pages
Amsterdam: Elsevier, 2009. Vol. 143, no 1-2, 102-105 p.
Optical tweezers, Single bond dissociation, Receptor–ligand interaction, Bond strength, Lewis b receptor
Physical Sciences Biochemistry and Molecular Biology
Research subject Physics
IdentifiersURN: urn:nbn:se:umu:diva-21486DOI: 10.1016/j.bpc.2009.03.007ISI: 000267006000012OAI: oai:DiVA.org:umu-21486DiVA: diva2:211326